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Golgi apparatus

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289:("internal reticular apparatus"). Some doubted the discovery at first, arguing that the appearance of the structure was merely an optical illusion created by the observation technique used by Golgi. With the development of modern microscopes in the twentieth century, the discovery was confirmed. Early references to the Golgi apparatus referred to it by various names including the "Golgi–Holmgren apparatus", "Golgi–Holmgren ducts", and "Golgi–Kopsch apparatus". The term "Golgi apparatus" was used in 1910 and first appeared in the scientific literature in 1913, while "Golgi complex" was introduced in 1956. 36: 1081: 348: 605: 1947: 66: 1972: 930:. Additionally, tubular connections are not prevalent in plant cells. The roles that these connections have can be attributed to a cell-specific specialization rather than a universal trait. If the membranes are continuous, that suggests the existence of mechanisms that preserve the unique biochemical gradients observed throughout the Golgi apparatus. 1047: 474: 942:
This rapid partitioning model is the most drastic alteration of the traditional vesicular trafficking point of view. Proponents of this model hypothesize that the Golgi works as a single unit, containing domains that function separately in the processing and export of protein cargo. Cargo from the ER
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Vesicles contain proteins destined for extracellular release. After packaging, the vesicles bud off and are stored in the cell until a signal is given for their release. When the appropriate signal is received they move toward the membrane and fuse to release their contents. This process is known as
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This model cannot explain the transport kinetics of large protein cargo, such as collagen. This model falls short on explaining the observation of discrete compartments and polarized biochemistry of the Golgi cisternae. It also does not explain formation and disintegration of the Golgi network, nor
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The model addresses the existence of Golgi compartments, as well as differing biochemistry within the cisternae, transport of large proteins, transient formation and disintegration of the cisternae, and retrograde mobility of native Golgi proteins, and it can account for the variability seen in the
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of the Golgi stack, which progresses later to become mature TGN cisternae. Once matured, the TGN cisternae dissolve to become secretory vesicles. While this progression occurs, COPI vesicles continually recycle Golgi-specific proteins by delivery from older to younger cisternae. Different recycling
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This model does not explain morphological variations in the Golgi apparatus, nor define a role for COPI vesicles. This model does not apply well for plants, algae, and fungi in which individual Golgi stacks are observed (transfer of domains between stacks is not likely). Additionally, megavesicles
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This model is an extension of the cisternal progression/maturation model. It incorporates the existence of tubular connections among the cisternae that form the Golgi ribbon, in which cisternae within a stack are linked. This model posits that the tubules are important for bidirectional traffic in
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responsible for selectively modifying protein cargo. These modifications influence the fate of the protein. The compartmentalization of the Golgi apparatus is advantageous for separating enzymes, thereby maintaining consecutive and selective processing steps: enzymes catalyzing early modifications
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This model is consistent with numerous observations and encompasses some of the strengths of the cisternal progression/maturation model. Additionally, what is known of the Rab GTPase roles in mammalian endosomes can help predict putative roles within the Golgi. This model is unique in that it can
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move between these two domains, and randomly exit from any level of the Golgi to their final location. This model is supported by the observation that cargo exits the Golgi in a pattern best described by exponential kinetics. The existence of domains is supported by fluorescence microscopy data.
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Though there are multiple models that attempt to explain vesicular traffic throughout the Golgi, no individual model can independently explain all observations of the Golgi apparatus. Currently, the cisternal progression/maturation model is the most accepted among scientists, accommodating many
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Since the amount of COPI vesicles varies drastically among types of cells, this model cannot easily explain high trafficking activity within the Golgi for both small and large cargoes. Additionally, there is no convincing evidence that COPI vesicles move in both the anterograde and retrograde
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The structure and function of the Golgi apparatus are intimately linked. Individual stacks have different assortments of enzymes, allowing for progressive processing of cargo proteins as they travel from the cisternae to the trans Golgi face. Enzymatic reactions within the Golgi stacks occur
1051: 1050: 1065: 1052: 1000:. The other models are still important in framing questions and guiding future experimentation. Among the fundamental unanswered questions are the directionality of COPI vesicles and role of Rab GTPases in modulating protein cargo traffic. 1049: 1080: 683:(TGN). This area of the Golgi is the point at which proteins are sorted and shipped to their intended destinations by their placement into one of at least three different types of vesicles, depending upon the 1035:(GEFs) that mediate GTP-binding of ARFs. Treatment of cells with BFA thus disrupts the secretion pathway, promoting disassembly of the Golgi apparatus and distributing Golgi proteins to the endosomes and ER. 920:
This model encompasses the strengths of the cisternal progression/maturation model that also explains rapid trafficking of cargo, and how native Golgi proteins can recycle independently of COPI vesicles.
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patterns may account for the differing biochemistry throughout the Golgi stack. Thus, the compartments within the Golgi are seen as discrete kinetic stages of the maturing Golgi apparatus.
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or for use in the cell. In this respect, the Golgi can be thought of as similar to a post office: it packages and labels items which it then sends to different parts of the cell or to the
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The model explains observations of compartments, polarized distribution of enzymes, and waves of moving vesicles. It also attempts to explain how Golgi-specific enzymes are recycled.
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This model cannot easily explain the observation of fused Golgi networks, tubular connections among cisternae, and differing kinetics of secretory cargo exit.
399:, secretory vesicles, or the cell surface. The TGN is usually positioned adjacent to the stack, but can also be separate from it. The TGN may act as an early 313:. In experiments it is seen that as microtubules are depolymerized the Golgi apparatuses lose mutual connections and become individual stacks throughout the 509:
exclusively near its membrane surfaces, where enzymes are anchored. This feature is in contrast to the ER, which has soluble proteins and enzymes in its
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In most eukaryotes, the Golgi apparatus is made up of a series of compartments and is a collection of fused, flattened membrane-enclosed disks known as
367:. A mammalian cell typically contains 40 to 100 stacks of cisternae. Between four and eight cisternae are usually present in a stack; however, in some 1064: 309:. Tubular connections are responsible for linking the stacks together. Localization and tubular connections of the Golgi apparatus are dependent on 2426: 780:, or to lysosome-like storage organelles. These proteins include both digestive enzymes and membrane proteins. The vesicle first fuses with the 2004: 414:
There are structural and organizational differences in the Golgi apparatus among eukaryotes. In some yeasts, Golgi stacking is not observed.
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The Golgi apparatus tends to be larger and more numerous in cells that synthesize and secrete large amounts of substances; for example, the
1246: 331:, Golgi stacks are not concentrated at the centrosomal region and do not form Golgi ribbons. Organization of the plant Golgi depends on 914:
the ER-Golgi system: they allow for fast anterograde traffic of small cargo and/or the retrograde traffic of native Golgi proteins.
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In this model, the Golgi is viewed as a set of stable compartments that work together. Each compartment has a unique collection of
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inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and
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Notably, this model explains the exponential kinetics of cargo exit of both large and small proteins, whereas other models cannot.
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Fabene PF, Bentivoglio M (October 1998). "1898-1998: Camillo Golgi and "the Golgi": one hundred years of terminological clones".
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used experimentally to disrupt the secretion pathway as a method of testing Golgi function. BFA blocks the activation of some
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occurs within the TGN. Other general post-translational modifications of proteins include the addition of carbohydrates (
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This is the most recent model. In this model, the Golgi is seen as a collection of stable compartments defined by
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Duran JM, Kinseth M, Bossard C, Rose DW, Polishchuk R, Wu CC, Yates J, Zimmerman T, Malhotra V (June 2008).
1990: 664:. Once inside the lumen, the molecules are modified, then sorted for transport to their next destinations. 110: 94: 660:
face of the Golgi apparatus, where they fuse with the Golgi membrane and empty their contents into the
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The Golgi apparatus is a major collection and dispatch station of protein products received from the
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does not. In plants, the individual stacks of the Golgi apparatus seem to operate independently.
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D'Souza-Schorey C, Chavrier P (May 2006). "ARF proteins: roles in membrane traffic and beyond".
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as many as sixty cisternae have been observed. This collection of cisternae is broken down into
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that determines the final destination of the protein. For example, the Golgi apparatus adds a
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Owing to its large size and distinctive structure, the Golgi apparatus was one of the first
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that attach various sugar monomers to proteins as the proteins move through the apparatus.
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In this model, the fusion of COPII vesicles from the ER begins the formation of the first
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cables and not microtubules. The common feature among Golgi is that they are adjacent to
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to be discovered and observed in detail. It was discovered in 1898 by Italian physician
1919: 1892: 1873: 1818: 1793: 1766: 1741: 1717: 1692: 1531: 1506: 1471: 1446: 1422: 1397: 1183: 805: 1982: 1171: 387:(TGN). The CGN is the first cisternal structure, and the TGN is the final, from which 2350: 2188: 2071: 1924: 1865: 1823: 1771: 1757: 1722: 1640: 1594: 1567: 1536: 1476: 1427: 1378: 1373: 1356: 1337: 1291: 1284: 1187: 1175: 1129: 844: 747: 720: 585: 225: 1877: 321:, multiple Golgi apparatuses are scattered throughout the cytoplasm (as observed in 257:
The Golgi apparatus was identified in 1898 by the Italian biologist and pathologist
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This model cannot explain the transport kinetics of large protein cargo, such as
839:-coated vesicles. This model proposes that COPI vesicles move in two directions: 715: 661: 565: 518: 510: 416: 2210: 1708: 1556: 784:, and the contents are then transferred to the lysosome via unknown mechanisms. 714:
release. After packaging, the vesicles bud off and immediately move towards the
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The Golgi Apparatus: State of the art 110 years after Camillo Golgi's discovery
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face, to a complex network of membranes and associated vesicles known as the
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Model 3: Cisternal progression/maturation with heterotypic tubular transport
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This model was widely accepted from the early 1980s until the late 1990s.
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face cisternae, and enzymes catalyzing later modifications are found in
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Yeast Golgi dynamics. Green labels early Golgi, red labels late Golgi.
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The Golgi apparatus (salmon pink) in context of the secretory pathway
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which regulate vesicular trafficking through the binding of COPs to
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Model 1: Anterograde vesicular transport between stable compartments
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Those proteins destined for areas of the cell other than either the
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Two Golgi stacks connected as a ribbon in a mouse cell. Taken from
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Three-dimensional projection of a mammalian Golgi stack imaged by
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exit face. These faces are characterized by unique morphology and
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explain the observation of "megavesicle" transport intermediates.
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The subcellular localization of the Golgi apparatus varies among
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Marie M, Sannerud R, Avsnes Dale H, Saraste J (September 2008).
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Nakano A, Luini A (August 2010). "Passage through the Golgi".
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Day, Kasey J.; Casler, Jason C.; Glick, Benjamin S. (2018).
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Pavelk M, Mironov AA (2008). "Golgi apparatus inheritance".
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Model 5: Stable compartments as cisternal model progenitors
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Vesicles contain proteins and ribosomes destined for the
173: 1794:"Take the 'A' train: on fast tracks to the cell surface" 261:. The organelle was later named after him in the 1910s. 2012: 1893:"COPI selectively drives maturation of the early Golgi" 1890: 1395: 485:(ER). Proteins synthesized in the ER are packaged into 239:
pathways. It is of particular importance in processing
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vesicles recycle Golgi-specific trafficking proteins.
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residues. Removal of mannose residues and addition of
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Current models of vesicular transport and trafficking
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of the immune system have prominent Golgi complexes.
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and the Golgi. BFA inhibits the function of several
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Bollettino della Società Medico-Chirurgica di Pavia
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are not established to be intra-Golgi transporters.
671:or the Golgi apparatus are moved through the Golgi 170: 1555: 1283: 1693:"Models for Golgi traffic: a critical assessment" 1586: 1500: 1447:"Budding Yeast Has a Minimal Endomembrane System" 1157: 819:cargo. Proteins are delivered from the ER to the 2413: 1891:Papanikou E, Day KJ, Austin J, Glick BS (2015). 1686: 1684: 1682: 1680: 1678: 1676: 1674: 1232: 1230: 1109: 16:Cell organelle that packages proteins for export 1843: 1841: 1839: 1837: 1787: 1785: 1672: 1670: 1668: 1666: 1664: 1662: 1660: 1658: 1656: 1654: 1496: 1494: 1492: 1490: 521:on lysosomal proteins occurs in the early CGN. 379:compartments, making up two main networks: the 1444: 1315: 1313: 1311: 1309: 1307: 1203:"Intorno alla struttura delle cellule nervose" 452:. Within individual stacks are assortments of 440:In all eukaryotes, each cisternal stack has a 1998: 1227: 1153: 1151: 1149: 1147: 1145: 1115: 517:of proteins. For example, phosphorylation of 1884: 1834: 1782: 1651: 1614: 1487: 937:Model 4: Rapid partitioning in a mixed Golgi 1438: 1389: 1348: 1319: 1304: 1236: 292: 2005: 1991: 1739: 1697:Cold Spring Harbor Perspectives in Biology 1690: 1620: 1580: 1354: 1142: 612:(orange) to Golgi apparatus (magenta). 1. 584:. Enzymes in the Golgi append proteins to 497:. The Golgi apparatus is also involved in 1918: 1908: 1817: 1765: 1716: 1634: 1530: 1470: 1421: 1372: 1277: 1275: 1273: 1271: 1269: 1267: 1265: 1263: 874:Model 2: Cisternal progression/maturation 1623:"Synthesis and sorting of proteoglycans" 1553: 1547: 603: 472: 346: 34: 1281: 710:Vesicle contains proteins destined for 536:occur in medial cisternae. Addition of 2427:Anatomy named for one who described it 2414: 1850:Nature Reviews. Molecular Cell Biology 1260: 599: 513:. Much of the enzymatic processing is 1986: 1200: 281:. After first observing it under his 70:Components of a typical animal cell: 1798:Cellular and Molecular Life Sciences 1282:Alberts, Bruce; et al. (1994). 568:). Protein modifications may form a 465:face cisternae of the Golgi stacks. 39:Diagram of a single "stack" of Golgi 1740:Wei JH, Seemann J (November 2010). 1733: 1691:Glick BS, Luini A (November 2011). 1033:guanine nucleotide exchange factors 528:are associated with the removal of 13: 1621:Prydz K, Dalen KT (January 2000). 1090:and volume surface rendered using 608:Diagram of secretory process from 14: 2438: 1938: 1593:. Nova Publishers. pp. 45–. 1120:. Berlin: Springer. p. 580. 831:. Cargo then progress toward the 1970: 1945: 1758:10.1111/j.1600-0854.2010.01114.x 1590:Biotechnology and Bioengineering 1374:10.1111/j.1600-0854.2011.01316.x 1223:from the original on 2018-04-07. 1079: 1063: 1045: 166: 64: 1511:Histochemistry and Cell Biology 1355:Suda Y, Nakano A (April 2012). 1322:Current Opinion in Cell Biology 1249:from the original on 2006-11-07 576:label to proteins destined for 515:post-translational modification 420:does have stacked Golgi, while 351:3D rendering of Golgi apparatus 277:during an investigation of the 1629:. 113. 113 Pt 2 (2): 193–205. 1194: 1003: 1: 2169:Microtubule organizing center 1742:"Unraveling the Golgi ribbon" 1505:, Glick BS (September 2013). 1402:Molecular Biology of the Cell 1286:Molecular Biology of the Cell 1172:10.1016/S0361-9230(98)00079-3 1103: 640:face of Golgi apparatus; 11. 636:face of Golgi apparatus; 10. 285:, he termed the structure as 1463:10.1016/j.devcel.2017.12.014 1245:. Florida State University. 1126:10.1007/978-3-211-76310-0_34 342: 264: 111:Smooth endoplasmic reticulum 7: 1709:10.1101/cshperspect.a005215 1357:"The yeast Golgi apparatus" 654:rough endoplasmic reticulum 468: 287:apparato reticolare interno 95:Rough endoplasmic reticulum 10: 2443: 1587:William G. Flynne (2008). 1237:Davidson MW (2004-12-13). 1038: 956:the role of COPI vesicles. 18: 2388: 2323: 2248: 2139: 2025: 1810:10.1007/s00018-008-8355-0 1554:Campbell, Neil A (1996). 1523:10.1007/s00418-013-1128-3 1334:10.1016/j.ceb.2010.05.003 632:; 8. Golgi apparatus; 9. 592:molecules present in the 63: 54: 45: 2164:Prokaryotic cytoskeleton 895:structures of the Golgi. 423:Saccharomyces cerevisiae 324:Saccharomyces cerevisiae 293:Subcellular localization 132:; with which, comprises 20:Not to be confused with 1627:Journal of Cell Science 1414:10.1091/mbc.E07-10-0998 1160:Brain Research Bulletin 656:are transported to the 644:of the Golgi apparatus. 1290:. Garland Publishing. 721:constitutive secretion 645: 478: 352: 247:, containing a set of 40: 2154:Intermediate filament 2047:Endoplasmic reticulum 1636:10.1242/jcs.113.2.193 1243:Molecular Expressions 1239:"The Golgi Apparatus" 1094:software. Taken from 776:containing many acid 730:release by activated 669:endoplasmic reticulum 610:endoplasmic reticulum 607: 483:endoplasmic reticulum 476: 365:endoplasmic reticulum 350: 337:endoplasmic reticulum 193:), also known as the 128:(fluid that contains 38: 2401:Extracellular matrix 1979:at Wikimedia Commons 996:observations across 815:that work to modify 704:Exocytotic vesicles 624:attached to RER; 6. 594:extracellular matrix 457:are gathered in the 2104:Cytoplasmic granule 1910:10.7554/eLife.13232 1088:confocal microscopy 765:Lysosomal vesicles 748:regulated secretion 738:Secretory vesicles 681:trans-Golgi network 600:Vesicular transport 574:mannose-6-phosphate 534:N-acetylglucosamine 495:extracellular space 385:trans Golgi network 218:endomembrane system 86:(dots as part of 5) 57:Animal cell diagram 2129:Weibel–Palade body 2013:Structures of the 1955:has a profile for 1451:Developmental Cell 1023:). ARFs are small 1011:(BFA) is a fungal 845:secretory proteins 646: 586:glycosaminoglycans 564:) and phosphates ( 479: 391:are packaged into 353: 41: 27:For the song, see 2409: 2408: 2189:Spindle pole body 1975:Media related to 1961: 1600:978-1-60456-067-1 1573:978-0-8053-1957-6 1297:978-0-8153-1619-0 1135:978-3-211-76310-0 1053: 798: 797: 791:destined for the 444:entry face and a 381:cis Golgi network 339:(ER) exit sites. 226:packages proteins 158: 157: 2434: 2007: 2000: 1993: 1984: 1983: 1974: 1959: 1958:Golgi apparatus 1949: 1948: 1933: 1932: 1922: 1912: 1888: 1882: 1881: 1845: 1832: 1831: 1821: 1789: 1780: 1779: 1769: 1752:(11): 1391–400. 1737: 1731: 1730: 1720: 1688: 1649: 1648: 1638: 1618: 1612: 1611: 1609: 1607: 1584: 1578: 1577: 1561: 1551: 1545: 1544: 1534: 1498: 1485: 1484: 1474: 1442: 1436: 1435: 1425: 1393: 1387: 1386: 1376: 1352: 1346: 1345: 1317: 1302: 1301: 1289: 1279: 1258: 1257: 1255: 1254: 1234: 1225: 1224: 1222: 1207: 1201:Golgi C (1898). 1198: 1192: 1191: 1155: 1140: 1139: 1113: 1083: 1067: 1055: 1054: 1017:ADP-ribosylation 772:, a degradative 755:Neurotransmitter 690: 689: 614:Nuclear membrane 519:oligosaccharides 201:, or simply the 192: 191: 188: 187: 184: 181: 178: 175: 172: 102:(or, Golgi body) 68: 58: 49: 43: 42: 32: 25: 2442: 2441: 2437: 2436: 2435: 2433: 2432: 2431: 2412: 2411: 2410: 2405: 2384: 2319: 2244: 2135: 2052:Golgi apparatus 2028: 2021: 2011: 1977:Golgi apparatus 1967: 1966: 1965: 1950: 1946: 1941: 1936: 1889: 1885: 1862:10.1038/nrm1910 1846: 1835: 1804:(18): 2859–74. 1790: 1783: 1738: 1734: 1703:(11): a005215. 1689: 1652: 1619: 1615: 1605: 1603: 1601: 1585: 1581: 1574: 1552: 1548: 1499: 1488: 1457:(1): 56–72.e4. 1443: 1439: 1394: 1390: 1353: 1349: 1318: 1305: 1298: 1280: 1261: 1252: 1250: 1235: 1228: 1220: 1205: 1199: 1195: 1156: 1143: 1136: 1114: 1110: 1106: 1099: 1084: 1075: 1068: 1059: 1056: 1046: 1041: 1006: 970:Rab (G-protein) 965: 939: 910: 876: 843:vesicles carry 808: 803: 716:plasma membrane 685:signal sequence 652:that leave the 628:; 7. Transport 602: 570:signal sequence 566:phosphorylation 471: 417:Pichia pastoris 345: 305:, close to the 295: 267: 169: 165: 162:Golgi apparatus 154: 100:Golgi apparatus 56: 47: 33: 26: 19: 17: 12: 11: 5: 2440: 2430: 2429: 2424: 2407: 2406: 2404: 2403: 2398: 2392: 2390: 2386: 2385: 2383: 2382: 2377: 2372: 2371: 2370: 2365: 2355: 2354: 2353: 2348: 2343: 2333: 2327: 2325: 2324:Other internal 2321: 2320: 2318: 2317: 2312: 2311: 2310: 2305: 2300: 2295: 2290: 2285: 2280: 2275: 2270: 2260: 2254: 2252: 2246: 2245: 2243: 2242: 2241: 2240: 2235: 2225: 2224: 2223: 2218: 2213: 2208: 2198: 2193: 2192: 2191: 2186: 2181: 2176: 2166: 2161: 2156: 2151: 2145: 2143: 2137: 2136: 2134: 2133: 2132: 2131: 2126: 2121: 2116: 2111: 2101: 2100: 2099: 2094: 2089: 2084: 2079: 2074: 2064: 2059: 2054: 2049: 2044: 2039: 2033: 2031: 2023: 2022: 2010: 2009: 2002: 1995: 1987: 1981: 1980: 1951: 1944: 1943: 1942: 1940: 1939:External links 1937: 1935: 1934: 1883: 1833: 1781: 1732: 1650: 1613: 1599: 1579: 1572: 1546: 1486: 1437: 1408:(6): 2579–87. 1388: 1347: 1303: 1296: 1259: 1226: 1193: 1141: 1134: 1107: 1105: 1102: 1101: 1100: 1085: 1078: 1076: 1069: 1062: 1060: 1057: 1044: 1040: 1037: 1005: 1002: 993: 992: 991: 990: 983: 964: 961: 960: 959: 958: 957: 950: 938: 935: 934: 933: 932: 931: 921: 909: 906: 905: 904: 903: 902: 896: 875: 872: 871: 870: 867: 866: 865: 858: 807: 804: 802: 799: 796: 795: 785: 766: 762: 761: 752: 742: 735: 734: 732:plasma B cells 725: 708: 706:(constitutive) 701: 700: 697: 694: 626:Macromolecules 601: 598: 590:polysaccharide 544:occurs in the 501:transport and 470: 467: 435:plasma B cells 383:(CGN) and the 375:, medial, and 344: 341: 294: 291: 279:nervous system 266: 263: 230:membrane-bound 216:. Part of the 209:found in most 156: 155: 153: 152: 147: 142: 137: 123: 118: 113: 108: 103: 97: 92: 87: 81: 76: 69: 61: 60: 52: 51: 15: 9: 6: 4: 3: 2: 2439: 2428: 2425: 2423: 2420: 2419: 2417: 2402: 2399: 2397: 2394: 2393: 2391: 2387: 2381: 2378: 2376: 2373: 2369: 2366: 2364: 2361: 2360: 2359: 2356: 2352: 2349: 2347: 2344: 2342: 2339: 2338: 2337: 2334: 2332: 2329: 2328: 2326: 2322: 2316: 2313: 2309: 2306: 2304: 2301: 2299: 2298:Proteinoplast 2296: 2294: 2291: 2289: 2286: 2284: 2281: 2279: 2276: 2274: 2271: 2269: 2266: 2265: 2264: 2261: 2259: 2258:Mitochondrion 2256: 2255: 2253: 2251: 2250:Endosymbionts 2247: 2239: 2236: 2234: 2233:Lamellipodium 2231: 2230: 2229: 2226: 2222: 2219: 2217: 2214: 2212: 2209: 2207: 2204: 2203: 2202: 2199: 2197: 2194: 2190: 2187: 2185: 2182: 2180: 2177: 2175: 2172: 2171: 2170: 2167: 2165: 2162: 2160: 2157: 2155: 2152: 2150: 2149:Microfilament 2147: 2146: 2144: 2142: 2138: 2130: 2127: 2125: 2122: 2120: 2117: 2115: 2112: 2110: 2107: 2106: 2105: 2102: 2098: 2095: 2093: 2090: 2088: 2085: 2083: 2080: 2078: 2075: 2073: 2070: 2069: 2068: 2065: 2063: 2062:Autophagosome 2060: 2058: 2055: 2053: 2050: 2048: 2045: 2043: 2040: 2038: 2037:Cell membrane 2035: 2034: 2032: 2030: 2027:Endomembrane 2024: 2020: 2016: 2008: 2003: 2001: 1996: 1994: 1989: 1988: 1985: 1978: 1973: 1969: 1968: 1963: 1962: 1954: 1930: 1926: 1921: 1916: 1911: 1906: 1902: 1898: 1894: 1887: 1879: 1875: 1871: 1867: 1863: 1859: 1856:(5): 347–58. 1855: 1851: 1844: 1842: 1840: 1838: 1829: 1825: 1820: 1815: 1811: 1807: 1803: 1799: 1795: 1788: 1786: 1777: 1773: 1768: 1763: 1759: 1755: 1751: 1747: 1743: 1736: 1728: 1724: 1719: 1714: 1710: 1706: 1702: 1698: 1694: 1687: 1685: 1683: 1681: 1679: 1677: 1675: 1673: 1671: 1669: 1667: 1665: 1663: 1661: 1659: 1657: 1655: 1646: 1642: 1637: 1632: 1628: 1624: 1617: 1602: 1596: 1592: 1591: 1583: 1575: 1569: 1565: 1560: 1559: 1550: 1542: 1538: 1533: 1528: 1524: 1520: 1517:(3): 239–49. 1516: 1512: 1508: 1504: 1497: 1495: 1493: 1491: 1482: 1478: 1473: 1468: 1464: 1460: 1456: 1452: 1448: 1441: 1433: 1429: 1424: 1419: 1415: 1411: 1407: 1403: 1399: 1392: 1384: 1380: 1375: 1370: 1367:(4): 505–10. 1366: 1362: 1358: 1351: 1343: 1339: 1335: 1331: 1327: 1323: 1316: 1314: 1312: 1310: 1308: 1299: 1293: 1288: 1287: 1278: 1276: 1274: 1272: 1270: 1268: 1266: 1264: 1248: 1244: 1240: 1233: 1231: 1219: 1215: 1211: 1204: 1197: 1189: 1185: 1181: 1177: 1173: 1169: 1165: 1161: 1154: 1152: 1150: 1148: 1146: 1137: 1131: 1127: 1123: 1119: 1112: 1108: 1097: 1093: 1089: 1082: 1077: 1073: 1066: 1061: 1043: 1042: 1036: 1034: 1030: 1026: 1022: 1018: 1014: 1010: 1001: 999: 987: 984: 980: 977: 976: 974: 971: 967: 966: 954: 951: 948: 945: 944: 941: 940: 929: 925: 922: 919: 916: 915: 912: 911: 900: 897: 893: 890: 889: 886: 882: 878: 877: 868: 862: 859: 856: 853: 852: 850: 846: 842: 838: 834: 830: 826: 822: 818: 814: 810: 809: 794: 790: 786: 783: 782:late endosome 779: 775: 771: 767: 764: 763: 760: 757:release from 756: 753: 750: 749: 743: 741: 737: 736: 733: 729: 726: 723: 722: 717: 713: 712:extracellular 709: 707: 703: 702: 698: 695: 692: 691: 688: 686: 682: 678: 674: 670: 665: 663: 659: 655: 651: 643: 639: 635: 631: 627: 623: 619: 615: 611: 606: 597: 595: 591: 587: 583: 582:proteoglycans 579: 575: 571: 567: 563: 562:glycosylation 559: 558:carbohydrates 555: 551: 547: 543: 539: 535: 531: 527: 524: 520: 516: 512: 506: 504: 500: 496: 492: 488: 484: 475: 466: 464: 460: 455: 451: 447: 443: 438: 436: 432: 427: 425: 424: 419: 418: 412: 410: 406: 402: 398: 394: 390: 386: 382: 378: 374: 370: 366: 362: 358: 349: 340: 338: 334: 330: 326: 325: 320: 316: 312: 308: 304: 300: 290: 288: 284: 280: 276: 275:Camillo Golgi 272: 262: 260: 259:Camillo Golgi 255: 253: 250: 249:glycosylation 246: 242: 238: 234: 231: 227: 223: 219: 215: 212: 208: 204: 200: 196: 195:Golgi complex 190: 163: 151: 150:Cell membrane 148: 146: 143: 141: 138: 135: 131: 127: 124: 122: 119: 117: 116:Mitochondrion 114: 112: 109: 107: 104: 101: 98: 96: 93: 91: 88: 85: 82: 80: 77: 75: 72: 71: 67: 62: 59: 53: 50: 44: 37: 30: 29:Junta (album) 23: 2278:Gerontoplast 2228:Pseudopodium 2221:Radial spoke 2201:Undulipodium 2141:Cytoskeleton 2057:Parenthesome 2051: 1957: 1900: 1896: 1886: 1853: 1849: 1801: 1797: 1749: 1745: 1735: 1700: 1696: 1626: 1616: 1604:. Retrieved 1589: 1582: 1557: 1549: 1514: 1510: 1503:Staehelin LA 1454: 1450: 1440: 1405: 1401: 1391: 1364: 1360: 1350: 1328:(4): 471–8. 1325: 1321: 1285: 1251:. Retrieved 1242: 1213: 1209: 1196: 1166:(3): 195–8. 1163: 1159: 1117: 1111: 1007: 994: 985: 978: 952: 946: 923: 917: 898: 891: 880: 860: 854: 832: 820: 746: 739: 719: 705: 696:Description 687:they carry. 680: 676: 675:towards the 666: 657: 647: 637: 633: 618:Nuclear pore 596:of animals. 545: 522: 507: 480: 462: 458: 450:biochemistry 445: 441: 439: 428: 421: 415: 413: 395:destined to 384: 380: 376: 372: 360: 354: 322: 311:microtubules 303:cell nucleus 296: 286: 268: 256: 202: 198: 194: 161: 159: 106:Cytoskeleton 99: 48:Cell biology 22:gyrification 2380:Magnetosome 2346:Spliceosome 2273:Chromoplast 2268:Chloroplast 2159:Microtubule 1606:13 November 1009:Brefeldin A 1004:Brefeldin A 986:Weaknesses: 953:Weaknesses: 924:Weaknesses: 899:Weaknesses: 864:directions. 861:Weaknesses: 841:anterograde 823:face using 740:(regulated) 548:cisternae. 542:sialic acid 505:formation. 433:-secreting 359:(singular: 2422:Organelles 2416:Categories 2375:Proteasome 2368:Inclusions 2315:Nitroplast 2308:Apicoplast 2293:Elaioplast 2288:Amyloplast 2283:Leucoplast 2238:Filopodium 2184:Basal body 2174:Centrosome 2124:Peroxisome 2119:Glyoxysome 2109:Melanosome 2019:organelles 1253:2010-09-20 1216:(1): 316. 1104:References 1013:metabolite 998:eukaryotes 979:Strengths: 947:Strengths: 918:Strengths: 892:Strengths: 855:Strengths: 849:retrograde 787:Digestive 778:hydrolases 491:exocytosis 307:centrosome 299:eukaryotes 283:microscope 271:organelles 211:eukaryotic 199:Golgi body 145:Centrosome 130:organelles 2396:Cell wall 2358:Cytoplasm 2331:Nucleolus 2303:Tannosome 2211:Flagellum 2196:Myofibril 2179:Centriole 2114:Microbody 2087:Phagosome 1188:208785591 1096:the movie 1072:the movie 1029:endosomes 1019:factors ( 789:proteases 774:organelle 673:cisternae 642:Cisternae 578:lysosomes 554:tyrosines 550:Sulfation 538:galactose 397:lysosomes 357:cisternae 343:Structure 315:cytoplasm 265:Discovery 245:secretion 237:endocytic 222:cytoplasm 207:organelle 134:cytoplasm 74:Nucleolus 2389:External 2341:Ribosome 2097:Acrosome 2082:Endosome 2077:Lysosome 1960:(Q83181) 1929:26709839 1878:19092867 1870:16633337 1828:18726174 1776:21040294 1727:21875986 1645:10633071 1541:23881164 1501:Day KJ, 1481:29316441 1432:18385516 1383:22132734 1342:20605430 1247:Archived 1218:Archived 928:collagen 885:cisterna 847:, while 835:face in 829:vesicles 827:-coated 793:lysosome 770:lysosome 728:Antibody 699:Example 650:vesicles 630:vesicles 622:Ribosome 526:cisterna 503:lysosome 487:vesicles 469:Function 431:antibody 401:endosome 393:vesicles 389:proteins 369:protists 361:cisterna 241:proteins 233:vesicles 205:, is an 140:Lysosome 84:Ribosome 2363:Cytosol 2263:Plastid 2216:Axoneme 2092:Vacuole 2072:Exosome 2067:Vesicle 2042:Nucleus 1953:Scholia 1920:4758959 1819:7079782 1767:4221251 1746:Traffic 1718:3220355 1566:, 123. 1558:Biology 1532:3779436 1472:5765772 1423:2397314 1361:Traffic 1180:9865849 1039:Gallery 1025:GTPases 973:GTPases 817:protein 813:enzymes 759:neurons 530:mannose 454:enzymes 252:enzymes 220:in the 126:Cytosol 121:Vacuole 90:Vesicle 79:Nucleus 2206:Cilium 2029:system 1927:  1917:  1876:  1868:  1826:  1816:  1774:  1764:  1725:  1715:  1643:  1597:  1570:  1539:  1529:  1479:  1469:  1430:  1420:  1381:  1340:  1294:  1186:  1178:  1132:  1092:Imaris 693:Types 409:plants 329:plants 327:). In 2351:Vault 1897:eLife 1874:S2CID 1221:(PDF) 1206:(PDF) 1184:S2CID 833:trans 825:COPII 677:trans 662:lumen 638:Trans 616:; 2. 546:trans 511:lumen 499:lipid 463:trans 446:trans 405:yeast 377:trans 333:actin 319:yeast 317:. In 228:into 224:, it 214:cells 203:Golgi 2015:cell 1925:PMID 1866:PMID 1824:PMID 1772:PMID 1723:PMID 1641:PMID 1608:2010 1595:ISBN 1568:ISBN 1537:PMID 1477:PMID 1428:PMID 1379:PMID 1338:PMID 1292:ISBN 1176:PMID 1130:ISBN 1021:ARFs 837:COPI 648:The 556:and 540:and 407:and 243:for 160:The 2336:RNA 1915:PMC 1905:doi 1858:doi 1814:PMC 1806:doi 1762:PMC 1754:doi 1713:PMC 1705:doi 1631:doi 1564:122 1527:PMC 1519:doi 1515:140 1467:PMC 1459:doi 1418:PMC 1410:doi 1369:doi 1330:doi 1168:doi 1122:doi 881:cis 821:cis 658:cis 634:Cis 552:of 523:Cis 459:cis 442:cis 403:in 373:cis 2418:: 2017:/ 1923:. 1913:. 1903:. 1899:. 1895:. 1872:. 1864:. 1852:. 1836:^ 1822:. 1812:. 1802:65 1800:. 1796:. 1784:^ 1770:. 1760:. 1750:11 1748:. 1744:. 1721:. 1711:. 1699:. 1695:. 1653:^ 1639:. 1625:. 1535:. 1525:. 1513:. 1509:. 1489:^ 1475:. 1465:. 1455:44 1453:. 1449:. 1426:. 1416:. 1406:19 1404:. 1400:. 1377:. 1365:13 1363:. 1359:. 1336:. 1326:22 1324:. 1306:^ 1262:^ 1241:. 1229:^ 1214:13 1212:. 1208:. 1182:. 1174:. 1164:47 1162:. 1144:^ 1128:. 1098:. 975:. 751:. 724:. 411:. 197:, 183:dʒ 2006:e 1999:t 1992:v 1964:. 1931:. 1907:: 1901:4 1880:. 1860:: 1854:7 1830:. 1808:: 1778:. 1756:: 1729:. 1707:: 1701:3 1647:. 1633:: 1610:. 1576:. 1543:. 1521:: 1483:. 1461:: 1434:. 1412:: 1385:. 1371:: 1344:. 1332:: 1300:. 1256:. 1190:. 1170:: 1138:. 1124:: 1074:. 883:- 189:/ 186:i 180:l 177:ɒ 174:ɡ 171:ˈ 168:/ 164:( 136:) 31:. 24:.

Index

gyrification
Junta (album)

Cell biology
Animal cell diagram

Nucleolus
Nucleus
Ribosome
Vesicle
Rough endoplasmic reticulum
Golgi apparatus
Cytoskeleton
Smooth endoplasmic reticulum
Mitochondrion
Vacuole
Cytosol
organelles
cytoplasm
Lysosome
Centrosome
Cell membrane
/ˈɡɒli/
organelle
eukaryotic
cells
endomembrane system
cytoplasm
packages proteins
membrane-bound

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