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Journal articles on the topic 'Golgi apparatus'

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Author: Grafiati

Published: 4 June 2021

Last updated: 25 May 2024

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1

Bucurica, Sandica, Laura Gaman, Mariana Jinga, Andrei Adrian Popa, and Florentina Ionita-Radu. "Golgi Apparatus Target Proteins in Gastroenterological Cancers: A Comprehensive Review of GOLPH3 and GOLGA Proteins." Cells 12, no. 14 (July 11, 2023): 1823. http://dx.doi.org/10.3390/cells12141823.

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The Golgi apparatus plays a central role in protein sorting, modification and trafficking within cells; its dysregulation has been implicated in various cancers including those affecting the GI tract. This review highlights two Golgi target proteins, namely GOLPH3 and GOLGA proteins, from this apparatus as they relate to gastroenterological cancers. GOLPH3—a highly conserved protein of the trans-Golgi network—has become a key player in cancer biology. Abnormal expression of GOLPH3 has been detected in various gastrointestinal cancers including gastric, colorectal and pancreatic cancers. GOLPH3 promotes tumor cell proliferation, survival, migration and invasion via various mechanisms including activating the PI3K/Akt/mTOR signaling pathway as well as altering Golgi morphology and vesicular trafficking. GOLGA family proteins such as GOLGA1 (golgin-97) and GOLGA7 (golgin-84) have also been implicated in gastroenterological cancers. GOLGA1 plays an essential role in protein trafficking within the Golgi apparatus and has been associated with poor patient survival rates and increased invasiveness; GOLGA7 maintains Golgi structure while having been shown to affect protein glycosylation processes. GOLPH3 and GOLGA proteins play a pivotal role in gastroenterological cancer, helping researchers unlock molecular mechanisms and identify therapeutic targets. Their dysregulation affects various cellular processes including signal transduction, vesicular trafficking and protein glycosylation, all contributing to tumor aggressiveness and progression.

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2

Diao, Aipo, Dinah Rahman, Darryl J. C. Pappin, John Lucocq, and Martin Lowe. "The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation." Journal of Cell Biology 160, no. 2 (January 20, 2003): 201–12. http://dx.doi.org/10.1083/jcb.200207045.

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Fragmentation of the mammalian Golgi apparatus during mitosis requires the phosphorylation of a specific subset of Golgi-associated proteins. We have used a biochemical approach to characterize these proteins and report here the identification of golgin-84 as a novel mitotic target. Using cryoelectron microscopy we could localize golgin-84 to the cis-Golgi network and found that it is enriched on tubules emanating from the lateral edges of, and often connecting, Golgi stacks. Golgin-84 binds to active rab1 but not cis-Golgi matrix proteins. Overexpression or depletion of golgin-84 results in fragmentation of the Golgi ribbon. Strikingly, the Golgi ribbon is converted into mini-stacks constituting only ∼25% of the volume of a normal Golgi apparatus upon golgin-84 depletion. These mini-stacks are able to carry out protein transport, though with reduced efficiency compared with a normal Golgi apparatus. Our results suggest that golgin-84 plays a key role in the assembly and maintenance of the Golgi ribbon in mammalian cells.

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3

Short, Benjamin, Christian Preisinger, Roman Körner, Robert Kopajtich, Olwyn Byron, and Francis A. Barr. "A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic." Journal of Cell Biology 155, no. 6 (December 10, 2001): 877–84. http://dx.doi.org/10.1083/jcb.200108079.

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Membrane traffic between the endoplasmic reticulum (ER) and Golgi apparatus and through the Golgi apparatus is a highly regulated process controlled by members of the rab GTPase family. The GTP form of rab1 regulates ER to Golgi transport by interaction with the vesicle tethering factor p115 and the cis-Golgi matrix protein GM130, also part of a complex with GRASP65 important for the organization of cis-Golgi cisternae. Here, we find that a novel coiled-coil protein golgin-45 interacts with the medial-Golgi matrix protein GRASP55 and the GTP form of rab2 but not other Golgi rab proteins. Depletion of golgin-45 disrupts the Golgi apparatus and causes a block in secretory protein transport. These results demonstrate that GRASP55 and golgin-45 form a rab2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure.

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4

Jiang, Shu, Sung W. Rhee, Paul A. Gleeson, and Brian Storrie. "Capacity of the Golgi Apparatus for Cargo Transport Prior to Complete Assembly." Molecular Biology of the Cell 17, no. 9 (September 2006): 4105–17. http://dx.doi.org/10.1091/mbc.e05-12-1112.

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In yeast, particular emphasis has been given to endoplasmic reticulum (ER)-derived, cisternal maturation models of Golgi assembly while in mammalian cells more emphasis has been given to golgins as a potentially stable assembly framework. In the case of de novo Golgi formation from the ER after brefeldin A/H89 washout in HeLa cells, we found that scattered, golgin-enriched, structures formed early and contained golgins including giantin, ranging across the entire cis to trans spectrum of the Golgi apparatus. These structures were incompetent in VSV-G cargo transport. Second, we compared Golgi competence in cargo transport to the kinetics of addition of various glycosyltransferases and glycosidases into nascent, golgin-enriched structures after drug washout. Enzyme accumulation was sequential with trans and then medial glycosyltransferases/glycosidases found in the scattered, nascent Golgi. Involvement in cargo transport preceded full accumulation of enzymes or GPP130 into nascent Golgi. Third, during mitosis, we found that the formation of a golgin-positive acceptor compartment in early telophase preceded the accumulation of a Golgi glycosyltransferase in nascent Golgi structures. We conclude that during mammalian Golgi assembly components fit into a dynamic, first-formed, multigolgin-enriched framework that is initially cargo transport incompetent. Resumption of cargo transport precedes full Golgi assembly.

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5

Yadav, Smita, Sapna Puri, and Adam D. Linstedt. "A Primary Role for Golgi Positioning in Directed Secretion, Cell Polarity, and Wound Healing." Molecular Biology of the Cell 20, no. 6 (March 15, 2009): 1728–36. http://dx.doi.org/10.1091/mbc.e08-10-1077.

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Peri-centrosomal positioning of the mammalian Golgi apparatus is known to involve microtubule-based motility, but its importance for cellular physiology is a major unanswered question. Here, we identify golgin-160 and GMAP210 as proteins required for centripetal motility of Golgi membranes. In the absence of either golgin, peri-centrosomal positioning of the Golgi apparatus was disrupted while the cytoskeleton remained intact. Although secretion persisted with normal kinetics, it was evenly distributed in response to wounding rather than directed to the wound edge. Strikingly, these cells also completely failed to polarize. Further, directionally persistent cell migration was inhibited such that wound closure was impaired. These findings not only reveal novel roles for golgin-160 and GMAP210 in conferring membrane motility but also indicate that Golgi positioning has an active role in directed secretion, cell polarity, and wound healing.

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6

Short, Ben, and Francis A. Barr. "The Golgi apparatus." Current Biology 10, no. 16 (August 2000): R583—R585. http://dx.doi.org/10.1016/s0960-9822(00)00644-8.

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7

Harris, Robin. "The Golgi apparatus." Micron 29, no. 2-3 (April 1998): 250. http://dx.doi.org/10.1016/s0968-4328(98)00005-5.

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8

Mărunţelu, Ion, Alexandra-Elena Constantinescu, Razvan-Adrian Covache-Busuioc, and Ileana Constantinescu. "The Golgi Apparatus: A Key Player in Innate Immunity." International Journal of Molecular Sciences 25, no. 7 (April 8, 2024): 4120. http://dx.doi.org/10.3390/ijms25074120.

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The Golgi apparatus, long recognized for its roles in protein processing and vesicular trafficking, has recently been identified as a crucial contributor to innate immune signaling pathways. This review discusses our expanding understanding of the Golgi apparatus’s involvement in initiating and activating these pathways. It highlights the significance of membrane connections between the Golgi and other organelles, such as the endoplasmic reticulum, mitochondria, endosomes, and autophagosomes. These connections are vital for the efficient transmission of innate immune signals and the activation of effector responses. Furthermore, the article delves into the Golgi apparatus’s roles in key immune pathways, including the inflammasome-mediated activation of caspase-1, the cGAS-STING pathway, and TLR/RLR signaling. Overall, this review aims to provide insights into the multifunctional nature of the Golgi apparatus and its impact on innate immunity.

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9

Liu, Chunyi, Mei Mei, Qiuling Li, Peristera Roboti, Qianqian Pang, Zhengzhou Ying, Fei Gao, Martin Lowe, and Shilai Bao. "Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice." Proceedings of the National Academy of Sciences 114, no. 2 (December 27, 2016): 346–51. http://dx.doi.org/10.1073/pnas.1608576114.

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The Golgi apparatus lies at the heart of the secretory pathway where it is required for secretory trafficking and cargo modification. Disruption of Golgi architecture and function has been widely observed in neurodegenerative disease, but whether Golgi dysfunction is causal with regard to the neurodegenerative process, or is simply a manifestation of neuronal death, remains unclear. Here we report that targeted loss of the golgin GM130 leads to a profound neurological phenotype in mice. Global KO of mouse GM130 results in developmental delay, severe ataxia, and postnatal death. We further show that selective deletion of GM130 in neurons causes fragmentation and defective positioning of the Golgi apparatus, impaired secretory trafficking, and dendritic atrophy in Purkinje cells. These cellular defects manifest as reduced cerebellar size and Purkinje cell number, leading to ataxia. Purkinje cell loss and ataxia first appear during postnatal development but progressively worsen with age. Our data therefore indicate that targeted disruption of the mammalian Golgi apparatus and secretory traffic results in neuronal degeneration in vivo, supporting the view that Golgi dysfunction can play a causative role in neurodegeneration.

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10

Sato, Keisuke, Peristera Roboti, Alexander A. Mironov, and Martin Lowe. "Coupling of vesicle tethering and Rab binding is required for in vivo functionality of the golgin GMAP-210." Molecular Biology of the Cell 26, no. 3 (February 2015): 537–53. http://dx.doi.org/10.1091/mbc.e14-10-1450.

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Golgins are extended coiled-coil proteins believed to participate in membrane-tethering events at the Golgi apparatus. However, the importance of golgin-mediated tethering remains poorly defined, and alternative functions for golgins have been proposed. Moreover, although golgins bind to Rab GTPases, the functional significance of Rab binding has yet to be determined. In this study, we show that depletion of the golgin GMAP-210 causes a loss of Golgi cisternae and accumulation of numerous vesicles. GMAP-210 function in vivo is dependent upon its ability to tether membranes, which is mediated exclusively by the amino-terminal ALPS motif. Binding to Rab2 is also important for GMAP-210 function, although it is dispensable for tethering per se. GMAP-210 length is also functionally important in vivo. Together our results indicate a key role for GMAP-210–mediated membrane tethering in maintaining Golgi structure and support a role for Rab2 binding in linking tethering with downstream docking and fusion events at the Golgi apparatus.

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11

Mazzarello, Paolo, and Marina Bentivoglio. "The centenarian Golgi apparatus." Nature 392, no. 6676 (April 1998): 543–44. http://dx.doi.org/10.1038/33266.

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12

Suda, Yasuyuki, and Akihiko Nakano. "The Yeast Golgi Apparatus." Traffic 13, no. 4 (December 27, 2011): 505–10. http://dx.doi.org/10.1111/j.1600-0854.2011.01316.x.

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13

Puthenveedu, Manojkumar A., and Adam D. Linstedt. "Subcompartmentalizing the Golgi apparatus." Current Opinion in Cell Biology 17, no. 4 (August 2005): 369–75. http://dx.doi.org/10.1016/j.ceb.2005.06.006.

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14

Linstedt, Adam D. "Positioning the Golgi Apparatus." Cell 118, no. 3 (August 2004): 271–72. http://dx.doi.org/10.1016/j.cell.2004.07.015.

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15

Morr�, D. James. "Golgi apparatus, cell wall." Protoplasma 180, no. 1-2 (March 1994): 1. http://dx.doi.org/10.1007/bf01379218.

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16

Mollenhauer, H. H., and D. J. Morr�. "Structure of Golgi apparatus." Protoplasma 180, no. 1-2 (March 1994): 14–28. http://dx.doi.org/10.1007/bf01379220.

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17

Dupree, Paul, and D. Janine Sherrier. "The plant Golgi apparatus." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1404, no. 1-2 (August 1998): 259–70. http://dx.doi.org/10.1016/s0167-4889(98)00061-5.

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18

Lu, Yiping, Wei Song, Zhiquan Tang, Wenru Shi, Shumei Gao, Jun Wu, Yuan Wang, Hu Pan, Yangang Wang, and Hong Huang. "The Preparation of Golgi Apparatus-Targeted Polymer Dots Encapsulated with Carbon Nanodots of Bright Near-Infrared Fluorescence for Long-Term Bioimaging." Molecules 28, no. 17 (August 31, 2023): 6366. http://dx.doi.org/10.3390/molecules28176366.

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As a vital organelle in eukaryotic cells, the Golgi apparatus is responsible for processing and transporting proteins in cells. Precisely monitoring the status of the Golgi apparatus with targeted fluorescence imaging technology is of enormous importance but remains a dramatically challenging task. In this study, we demonstrate the construction of the first Golgi apparatus-targeted near-infrared (NIR) fluorescent nanoprobe, termed Golgi-Pdots. As a starting point of our investigation, hydrophobic carbon nanodots (CNDs) with bright NIR fluorescence at 674 nm (fluorescence quantum yield: 12.18%), a narrow emission band of 23 nm, and excellent stability were easily prepared from Magnolia Denudata flowers using an ultrasonic method. Incorporating the CNDs into a polymer matrix modified with Golgi-targeting molecules allowed for the production of the water-soluble Golgi-Pdots, which showed high colloidal stability and similar optical properties compared with pristine CNDs. Further studies revealed that the Golgi-Pdots showed good biocompatibility and Golgi apparatus-targeting capability. Based on these fascinating merits, utilizing Golgi-Pdots for the long-term tracking of the Golgi apparatus inside live cells was immensely successful.

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19

Liu, Jianyang, Jialin He, Yan Huang, Han Xiao, Zheng Jiang, and Zhiping Hu. "The Golgi apparatus in neurorestoration." Journal of Neurorestoratology 7, no. 3 (2019): 116–28. http://dx.doi.org/10.26599/jnr.2019.9040017.

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The central role of the Golgi apparatus in critical cellular processes such as the transport, processing, and sorting of proteins and lipids has placed it at the forefront of cell science. Golgi apparatus dysfunction caused by primary defects within the Golgi or pharmacological and oxidative stress has been implicated in a wide range of neurodegenerative diseases. In addition to participating in disease progression, the Golgi apparatus plays pivotal roles in angiogenesis, neurogenesis, and synaptogenesis, thereby promoting neurological recovery. In this review, we focus on the functions of the Golgi apparatus and its mediated events during neurorestoration.

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20

Munro, S. "The Golgin Coiled-Coil Proteins of the Golgi Apparatus." Cold Spring Harbor Perspectives in Biology 3, no. 6 (March 23, 2011): a005256. http://dx.doi.org/10.1101/cshperspect.a005256.

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21

Preisinger, Christian, Benjamin Short, Veerle De Corte, Erik Bruyneel, Alexander Haas, Robert Kopajtich, Jan Gettemans, and Francis A. Barr. "YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3ζ." Journal of Cell Biology 164, no. 7 (March 22, 2004): 1009–20. http://dx.doi.org/10.1083/jcb.200310061.

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The Golgi apparatus has long been suggested to be important for directing secretion to specific sites on the plasma membrane in response to extracellular signaling events. However, the mechanisms by which signaling events are coordinated with Golgi apparatus function remain poorly understood. Here, we identify a scaffolding function for the Golgi matrix protein GM130 that sheds light on how such signaling events may be regulated. We show that the mammalian Ste20 kinases YSK1 and MST4 target to the Golgi apparatus via the Golgi matrix protein GM130. In addition, GM130 binding activates these kinases by promoting autophosphorylation of a conserved threonine within the T-loop. Interference with YSK1 function perturbs perinuclear Golgi organization, cell migration, and invasion into type I collagen. A biochemical screen identifies 14-3-3ζ as a specific substrate for YSK1 that localizes to the Golgi apparatus, and potentially links YSK1 signaling at the Golgi apparatus with protein transport events, cell adhesion, and polarity complexes important for cell migration.

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22

Benyair, Ron, Avital Eisenberg-Lerner, and Yifat Merbl. "Maintaining Golgi Homeostasis: A Balancing Act of Two Proteolytic Pathways." Cells 11, no. 5 (February 23, 2022): 780. http://dx.doi.org/10.3390/cells11050780.

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The Golgi apparatus is a central hub for cellular protein trafficking and signaling. Golgi structure and function is tightly coupled and undergoes dynamic changes in health and disease. A crucial requirement for maintaining Golgi homeostasis is the ability of the Golgi to target aberrant, misfolded, or otherwise unwanted proteins to degradation. Recent studies have revealed that the Golgi apparatus may degrade such proteins through autophagy, retrograde trafficking to the ER for ER-associated degradation (ERAD), and locally, through Golgi apparatus-related degradation (GARD). Here, we review recent discoveries in these mechanisms, highlighting the role of the Golgi in maintaining cellular homeostasis.

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23

Lauvrak, Silje U., Alicia Llorente, Tore-Geir Iversen, and Kirsten Sandvig. "Selective regulation of the Rab9-independent transport of ricin to the Golgi apparatus by calcium." Journal of Cell Science 115, no. 17 (September 1, 2002): 3449–56. http://dx.doi.org/10.1242/jcs.115.17.3449.

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Transport of ricin from endosomes to the Golgi apparatus occurs, in contrast to the transport of the mannose 6-phosphate receptor, by a Rab9-independent process. To characterize the pathway of ricin transport to the Golgi apparatus, we investigated whether it was regulated by calcium. As shown here, our data indicate that calcium is selectively involved in the regulation of ricin transport to the Golgi apparatus. Thapsigargin, which inhibits calcium transport into the ER, and the calcium ionophore A23187 both increased the transport of ricin to the Golgi apparatus by a factor of 20. By contrast, transport of the mannose 6-phosphate receptor to the Golgi apparatus was unaffected. Ricin and mannose 6-phosphate receptor transport were measured by quantifying the sulfation of modified forms of ricin and the mannose 6-phosphate receptor. The increased transport of ricin was reduced by wortmannin and LY294002, suggesting that phosphoinositide 3-kinase might be involved in transport of ricin to the Golgi apparatus. Together, these findings indicate that the different pathways to the Golgi apparatus utilized by ricin and the mannose 6-phosphate receptor are regulated by different mechanisms.

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24

Tamaki, Hideaki, and Shohei Yamashina. "Structural Integrity of the Golgi Stack Is Essential for Normal Secretory Functions of Rat Parotid Acinar Cells: Effects of Brefeldin A and Okadaic Acid." Journal of Histochemistry & Cytochemistry 50, no. 12 (December 2002): 1611–23. http://dx.doi.org/10.1177/002215540205001205.

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We examined the effects of specific inhibitors, brefeldin A (BFA) and okadaic acid (OA), on the ultrastructural organization of the Golgi apparatus and distributions of amylase, Golgi-associated proteins, and cathepsin D in the rat parotid acinar cells. BFA induced a rapid regression of the Golgi stack into rudimentary Golgi clusters composed of tubulovesicules, in parallel with a redistribution of the Golgi-resident proteins and a coat protein (β-COP) into the region of the rough endoplasmic reticulum (rER) or cytosol. The rapid disruption of the Golgi stack could also be induced by the effect of OA. However, redistribution of the Golgi proteins in rER or cytosol could not be observed and β-COP was not dispersed but was retained on the rudimentary Golgi apparatus. These findings suggested that the mechanism of OA in inducing degeneration of the Golgi stack was markedly different from that of BFA. In addition, missorting of amylase, a Golgi protein, and cathepsin D into incorrect transport pathways is apparent in the course of the disruption of the Golgi stack by OA. These Golgi-disrupting effects are reversible and the reconstruction of the stacked structure of the Golgi apparatus started immediately after the removal of inhibitors. In the recovery processes, missorting was also observed until the integrated structure of the Golgi apparatus was completely reconstructed. This suggested that the integrated structure of the Golgi apparatus was quite necessary for the occurrence of normal secretory events, including proper sorting of molecules.

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25

Ren, Xiaoyan, Anne G. Ostermeyer, Lynne T. Ramcharan, Youchun Zeng, Douglas M. Lublin, and Deborah A. Brown. "Conformational Defects Slow Golgi Exit, Block Oligomerization, and Reduce Raft Affinity of Caveolin-1 Mutant Proteins." Molecular Biology of the Cell 15, no. 10 (October 2004): 4556–67. http://dx.doi.org/10.1091/mbc.e04-06-0480.

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Caveolin-1, a structural protein of caveolae, is cleared unusually slowly from the Golgi apparatus during biosynthetic transport. Furthermore, several caveolin-1 mutant proteins accumulate in the Golgi apparatus. We examined this behavior further in this mutant study. Golgi accumulation probably resulted from loss of Golgi exit information, not exposure of cryptic retention signals, because several deletion mutants accumulated in the Golgi apparatus. Alterations throughout the protein caused Golgi accumulation. Thus, most probably acted indirectly, by affecting overall conformation, rather than by disrupting specific Golgi exit motifs. Consistent with this idea, almost all the Golgi-localized mutant proteins failed to oligomerize normally (even with an intact oligomerization domain), and they showed reduced raft affinity in an in vitro detergent-insolubility assay. A few mutant proteins formed unstable oligomers that migrated unusually slowly on blue native gels. Only one mutant protein, which lacked the first half of the N-terminal hydrophilic domain, accumulated in the Golgi apparatus despite normal oligomerization and raft association. These results suggested that transport of caveolin-1 through the Golgi apparatus is unusually difficult. The conformation of caveolin-1 may be optimized to overcome this difficulty, but remain very sensitive to mutation. Disrupting conformation can coordinately affect oligomerization, raft affinity, and Golgi exit of caveolin-1.

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26

Toader, Corneliu, Lucian Eva, Razvan-Adrian Covache-Busuioc, Horia Petre Costin, Luca-Andrei Glavan, Antonio Daniel Corlatescu, and Alexandru Vlad Ciurea. "Unraveling the Multifaceted Role of the Golgi Apparatus: Insights into Neuronal Plasticity, Development, Neurogenesis, Alzheimer’s Disease, and SARS-CoV-2 Interactions." Brain Sciences 13, no. 10 (September 23, 2023): 1363. http://dx.doi.org/10.3390/brainsci13101363.

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This article critically evaluates the multifunctional role of the Golgi apparatus within neurological paradigms. We succinctly highlight its influence on neuronal plasticity, development, and the vital trafficking and sorting mechanisms for proteins and lipids. The discourse further navigates to its regulatory prominence in neurogenesis and its implications in Alzheimer’s Disease pathogenesis. The emerging nexus between the Golgi apparatus and SARS-CoV-2 underscores its potential in viral replication processes. This consolidation accentuates the Golgi apparatus’s centrality in neurobiology and its intersections with both neurodegenerative and viral pathologies. In essence, understanding the Golgi’s multifaceted functions harbors profound implications for future therapeutic innovations in neurological and viral afflictions.

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27

Tassin, A. M., M. Paintrand, E. G. Berger, and M. Bornens. "The Golgi apparatus remains associated with microtubule organizing centers during myogenesis." Journal of Cell Biology 101, no. 2 (August 1, 1985): 630–38. http://dx.doi.org/10.1083/jcb.101.2.630.

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In vitro myogenesis involves a dramatic reorganization of the microtubular network, characterized principally by the relocalization of microtubule nucleating sites at the surface of the nuclei in myotubes, in marked contrast with the classical pericentriolar localization observed in myoblasts (Tassin, A. M., B. Maro, and M. Bornens, 1985, J. Cell Biol., 100:35-46). Since a spatial relationship between the Golgi apparatus and the centrosome is observed in most animal cells, we have decided to follow the fate of the Golgi apparatus during myogenesis by an immunocytochemical approach, using wheat germ agglutinin and an affinity-purified anti-galactosyltransferase. We show that Golgi apparatus in myotubes displays a perinuclear distribution which is strikingly different from the polarized juxtanuclear organization observed in myoblasts. As a result, the Golgi apparatus in myotubes is situated close to the microtubule organizing center (MTOC), the cis-side being situated at a fixed distance from the nuclear envelope, a situation which suggests the existence of a structural association between the Golgi apparatus and the nuclear periphery. This is supported by experiments of microtubule depolymerization by nocodazole, in which a minimal effect was observed on Golgi apparatus localization in myotubes in contrast with the dramatic scattering observed in myoblasts. In both cell types, electron microscopy reveals that microtubule disruption generates individual dictyosomes; this suggests that the connecting structures between dictyosomes are principally affected. This structural dependency of the Golgi apparatus upon microtubules is not apparently accompanied by a reverse dependency of MTOC structure or function upon Golgi apparatus activity. Golgi apparatus modification by monensin, as effective in myotubes as in myoblasts, is without apparent effect on MTOC localization or activity and on microtubule stability. The main result of our study is to show that in a cell type where the MTOC is dissociated from centrioles and where antero-posterior polarity has disappeared, the association between the Golgi apparatus and the MTOC is maintained. The significance of such a tight association is discussed.

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28

Futerman, A. H., and R. E. Pagano. "Determination of the intracellular sites and topology of glucosylceramide synthesis in rat liver." Biochemical Journal 280, no. 2 (December 1, 1991): 295–302. http://dx.doi.org/10.1042/bj2800295.

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We examined the intracellular site(s) and topology of glucosylceramide (GlcCer) synthesis in subcellular fractions from rat liver, using radioactive and fluorescent ceramide analogues as precursors, and compared these results with those obtained in our recent study of sphingomyelin (SM) synthesis in rat liver [Futerman, Stieger, Hubbard & Pagano (1990) J. Biol. Chem. 265, 8650-8657]. In contrast with SM synthesis, which occurs principally at the cis/medial Golgi apparatus, GlcCer synthesis was more widely distributed, with substantial amounts of synthesis detected in a heavy (cis/medial) Golgi-apparatus subfraction, a light smooth-vesicle fraction that is almost devoid of an endoplasmic-reticulum marker enzyme (glucose-6-phosphatase), and a heavy vesicle fraction. Furthermore, no GlcCer synthesis was detected in an enriched plasma-membrane fraction after accounting for contamination by Golgi-apparatus membranes. These results suggest that a significant amount of GlcCer may be synthesized in a pre- or early Golgi-apparatus compartment. Unlike SM synthesis, which occurs at the luminal surface of the Golgi apparatus, GlcCer synthesis appeared to occur at the cytosolic surface of intracellular membranes, since (i) limited proteolytic digestion of intact Golgi-apparatus vesicles almost completely inhibited GlcCer synthesis, and (ii) the extent of UDP-glucose translocation into the Golgi apparatus was insufficient to account for the amount of GlcCer synthesis measured. These findings imply that, after its synthesis, GlcCer must undergo transbilayer movement to the luminal surface to account for the known topology of higher-order glycosphingolipids within the Golgi apparatus and plasma membrane.

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29

Yang, Wuritu, Xiao-Juan Zhu, Jian Huang, Hui Ding, and Hao Lin. "A Brief Survey of Machine Learning Methods in Protein Sub-Golgi Localization." Current Bioinformatics 14, no. 3 (March 7, 2019): 234–40. http://dx.doi.org/10.2174/1574893613666181113131415.

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Background:The location of proteins in a cell can provide important clues to their functions in various biological processes. Thus, the application of machine learning method in the prediction of protein subcellular localization has become a hotspot in bioinformatics. As one of key organelles, the Golgi apparatus is in charge of protein storage, package, and distribution.Objective:The identification of protein location in Golgi apparatus will provide in-depth insights into their functions. Thus, the machine learning-based method of predicting protein location in Golgi apparatus has been extensively explored. The development of protein sub-Golgi apparatus localization prediction should be reviewed for providing a whole background for the fields.Method:The benchmark dataset, feature extraction, machine learning method and published results were summarized.Results:We briefly introduced the recent progresses in protein sub-Golgi apparatus localization prediction using machine learning methods and discussed their advantages and disadvantages.Conclusion:We pointed out the perspective of machine learning methods in protein sub-Golgi localization prediction.

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30

Le Bot, Nathalie, Claude Antony, Jamie White, Eric Karsenti, and Isabelle Vernos. "Role of Xklp3, a Subunit of the Xenopus Kinesin II Heterotrimeric Complex, in Membrane Transport between the Endoplasmic Reticulum and the Golgi Apparatus." Journal of Cell Biology 143, no. 6 (December 14, 1998): 1559–73. http://dx.doi.org/10.1083/jcb.143.6.1559.

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The function of the Golgi apparatus is to modify proteins and lipids synthesized in the ER and sort them to their final destination. The steady-state size and function of the Golgi apparatus is maintained through the recycling of some components back to the ER. Several lines of evidence indicate that the spatial segregation between the ER and the Golgi apparatus as well as trafficking between these two compartments require both microtubules and motors. We have cloned and characterized a new Xenopus kinesin like protein, Xklp3, a subunit of the heterotrimeric Kinesin II. By immunofluorescence it is found in the Golgi region. A more detailed analysis by EM shows that it is associated with a subset of membranes that contain the KDEL receptor and are localized between the ER and Golgi apparatus. An association of Xklp3 with the recycling compartment is further supported by a biochemical analysis and the behavior of Xklp3 in BFA-treated cells. The function of Xklp3 was analyzed by transfecting cells with a dominant-negative form lacking the motor domain. In these cells, the normal delivery of newly synthesized proteins to the Golgi apparatus is blocked. Taken together, these results indicate that Xklp3 is involved in the transport of tubular-vesicular elements between the ER and the Golgi apparatus.

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31

Grimmer, Stine, Tore-Geir Iversen, Bo van Deurs, and Kirsten Sandvig. "Endosome to Golgi Transport of Ricin Is Regulated by Cholesterol." Molecular Biology of the Cell 11, no. 12 (December 2000): 4205–16. http://dx.doi.org/10.1091/mbc.11.12.4205.

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We have here studied the role of cholesterol in transport of ricin from endosomes to the Golgi apparatus. Ricin is endocytosed even when cells are depleted for cholesterol by using methyl-β-cyclodextrin (mβCD). However, as here shown, the intracellular transport of ricin from endosomes to the Golgi apparatus, measured by quantifying sulfation of a modified ricin molecule, is strongly inhibited when the cholesterol content of the cell is reduced. On the other hand, increasing the level of cholesterol by treating cells with mβCD saturated with cholesterol (mβCD/chol) reduced the intracellular transport of ricin to the Golgi apparatus even more strongly. The intracellular transport routes affected include both Rab9-independent and Rab9-dependent pathways to the Golgi apparatus, since both sulfation of ricin after induced expression of mutant Rab9 (mRab9) to inhibit late endosome to Golgi transport and sulfation of a modified mannose 6-phosphate receptor (M6PR) were inhibited after removal or addition of cholesterol. Furthermore, the structure of the Golgi apparatus was affected by increased levels of cholesterol, as visualized by pronounced vesiculation and formation of smaller stacks. Thus, our results indicate that transport of ricin from endosomes to the Golgi apparatus is influenced by the cholesterol content of the cell.

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32

Fukunaga, T., M. Nagahama, K. Hatsuzawa, K. Tani, A. Yamamoto, and M. Tagaya. "Implication of sphingolipid metabolism in the stability of the Golgi apparatus." Journal of Cell Science 113, no. 18 (September 15, 2000): 3299–307. http://dx.doi.org/10.1242/jcs.113.18.3299.

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We examined the effects of short chain and long chain ceramides on the stability of the Golgi apparatus. Short chain ceramides, C(2)- and C(6)-ceramides, blocked brefeldin A-induced Golgi disassembly without affecting the rapid release of Golgi coat proteins, whereas they did not inhibit brefeldin A-induced tubulation of endosomes. Both short chain ceramides also retarded Golgi disassembly induced by nordihydroguaiaretic acid and nocodazole, suggesting that they stabilize the Golgi apparatus. In contrast to short chain ceramides, natural long chain ceramides, when incorporated into cells or formed within cells upon treatment with sphingomyelinase or metabolic inhibitors, enhanced brefeldin A-induced Golgi disassembly. These results suggest that sphingolipid metabolism is implicated in the stability of the Golgi apparatus.

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33

Wu, Y. N., M. Gadina, J. H. Tao-Cheng, and R. J. Youle. "Retinoic acid disrupts the Golgi apparatus and increases the cytosolic routing of specific protein toxins." Journal of Cell Biology 125, no. 4 (May 15, 1994): 743–53. http://dx.doi.org/10.1083/jcb.125.4.743.

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All-trans retinoic acid can specifically increase receptor mediated intoxication of ricin A chain immunotoxins more than 10,000 times, whereas fluid phase endocytosis of ricin A chain alone or ricin A chain immunotoxins was not influenced by retinoic acid. The immunotoxin activation by retinoic acid does not require RNA or protein synthesis and is not a consequence of increased receptor binding of the immunotoxin. Vitamin D3 and thyroid hormone T3, that activate retinoic acid receptor (RAR) cognates, forming heterodimers with retinoid X receptor (RXR), do not affect the potency of immunotoxins. Among other retinoids tested, 13-cis retinoic acid, which binds neither RAR nor RXR, also increases the potency of the ricin A chain immunotoxin. Therefore, retinoic acid receptor activation does not appear to be necessary for immunotoxin activity. Retinoic acid potentiation of immunotoxins is prevented by brefeldin A (BFA) indicating that in the presence of retinoic acid, the immunotoxin is efficiently routed through the Golgi apparatus en route to the cytoplasm. Directly examining cells with a monoclonal antibody (Mab) against mannosidase II, a Golgi apparatus marker enzyme, demonstrates that the Golgi apparatus changes upon treatment with retinoic acid from a perinuclear network to a diffuse aggregate. Within 60 min after removal of retinoic acid the cell reassembles the perinuclear Golgi network indistinguishable with that of normal control cells. C6-NBD-ceramide, a vital stain for the Golgi apparatus, shows that retinoic acid prevents the fluorescent staining of the Golgi apparatus and eliminates fluorescence of C6-NBD-ceramide prestained Golgi apparatus. Electron microscopy of retinoic acid-treated cells demonstrates the specific absence of any normal looking Golgi apparatus and a perinuclear vacuolar structure very similar to that seen in monensin-treated cells. This vacuolization disappears after removal of the retinoic acid and a perinuclear Golgi stacking reappears. These results indicate that retinoic acid alters intracellular routing, probably through the Golgi apparatus, potentiating immunotoxin activity indepedently of new gene expression. Retinoic acid appears to be a new reagent to manipulate the Golgi apparatus and intracellular traffic. As retinoic acid and immunotoxins are both in clinical trials for cancer therapy, their combined activity in vivo would be interesting to examine.

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34

Pelham, Hugh R. B. "Traffic through the Golgi apparatus." Journal of Cell Biology 155, no. 7 (December 24, 2001): 1099–102. http://dx.doi.org/10.1083/jcb.200110160.

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The role of vesicles in cargo transport through the Golgi apparatus has been controversial. Large forms of cargo such as protein aggregates are thought to progress through the Golgi stack by a process of cisternal maturation, balanced by a return flow of Golgi resident proteins in COPI-coated vesicles. However, whether this is the primary role of vesicles, or whether they also serve to transport small cargo molecules in a forward direction has been debated. Two papers (Martínez-Menárguez et al., 2001; Mironov et al., 2001, this issue) use sophisticated light and electron microscopy to provide evidence that the vesicular stomatitis virus membrane glycoprotein (VSV G)**Abbreviation used in this paper: VSV G, vesicular stomatitis virus membrane glycoprotein. is largely excluded from vesicles in vivo, and does not move between cisternae, whereas resident Golgi enzymes freely enter vesicles as predicted by the cisternal maturation model. Both papers conclude that vesicles are likely to play only a minor role in the anterograde transport of cargo through the Golgi apparatus in mammalian tissue culture cells.

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35

Siddhanta, Anirban, Andreea Radulescu, Michael C. Stankewich, Jon S. Morrow, and Dennis Shields. "Fragmentation of the Golgi Apparatus." Journal of Biological Chemistry 278, no. 3 (October 30, 2002): 1957–65. http://dx.doi.org/10.1074/jbc.m209137200.

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36

Jelerčič, U. "Mechanical model of Golgi apparatus." Physical Biology 16, no. 6 (September 5, 2019): 066003. http://dx.doi.org/10.1088/1478-3975/ab3766.

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37

Bretscher, M., and S. Munro. "Cholesterol and the Golgi apparatus." Science 261, no. 5126 (September 3, 1993): 1280–81. http://dx.doi.org/10.1126/science.8362242.

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38

Rios, Rosa M. "The centrosome–Golgi apparatus nexus." Philosophical Transactions of the Royal Society B: Biological Sciences 369, no. 1650 (September 5, 2014): 20130462. http://dx.doi.org/10.1098/rstb.2013.0462.

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A shared feature among all microtubule (MT)-dependent processes is the requirement for MTs to be organized in arrays of defined geometry. At a fundamental level, this is achieved by precisely controlling the timing and localization of the nucleation events that give rise to new MTs. To this end, MT nucleation is restricted to specific subcellular sites called MT-organizing centres. The primary MT-organizing centre in proliferating animal cells is the centrosome. However, the discovery of MT nucleation capacity of the Golgi apparatus (GA) has substantially changed our understanding of MT network organization in interphase cells. Interestingly, MT nucleation at the Golgi apparently relies on multiprotein complexes, similar to those present at the centrosome, that assemble at the cis -face of the organelle. In this process, AKAP450 plays a central role, acting as a scaffold to recruit other centrosomal proteins important for MT generation. MT arrays derived from either the centrosome or the GA differ in their geometry, probably reflecting their different, yet complementary, functions. Here, I review our current understanding of the molecular mechanisms involved in MT nucleation at the GA and how Golgi- and centrosome-based MT arrays work in concert to ensure the formation of a pericentrosomal polarized continuous Golgi ribbon structure, a critical feature for cell polarity in mammalian cells. In addition, I comment on the important role of the Golgi-nucleated MTs in organizing specialized MT arrays that serve specific functions in terminally differentiated cells.

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39

Barr, Francis. "The Golgi apparatus: an update." Trends in Cell Biology 12, no. 4 (April 2002): 161. http://dx.doi.org/10.1016/s0962-8924(02)02275-4.

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40

Glick, Benjamin S. "Organization of the Golgi apparatus." Current Opinion in Cell Biology 12, no. 4 (August 2000): 450–56. http://dx.doi.org/10.1016/s0955-0674(00)00116-2.

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41

Kondylis, Vangelis, and Catherine Rabouille. "The Golgi apparatus: Lessons fromDrosophila." FEBS Letters 583, no. 23 (October 1, 2009): 3827–38. http://dx.doi.org/10.1016/j.febslet.2009.09.048.

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42

Fan, Jie, Zhiping Hu, Liuwang Zeng, Wei Lu, Xiangqi Tang, Jie Zhang, and Ting Li. "Golgi apparatus and neurodegenerative diseases." International Journal of Developmental Neuroscience 26, no. 6 (May 23, 2008): 523–34. http://dx.doi.org/10.1016/j.ijdevneu.2008.05.006.

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43

Shanks, Ryan A., M. Cecilia Larocca, Mark Berryman, John C. Edwards, Tetsuro Urushidani, Jennifer Navarre, and James R. Goldenring. "AKAP350 at the Golgi Apparatus." Journal of Biological Chemistry 277, no. 43 (August 5, 2002): 40973–80. http://dx.doi.org/10.1074/jbc.m112277200.

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44

Shanks, Ryan A., Brent T. Steadman, P. Henry Schmidt, and James R. Goldenring. "AKAP350 at the Golgi Apparatus." Journal of Biological Chemistry 277, no. 43 (August 5, 2002): 40967–72. http://dx.doi.org/10.1074/jbc.m203307200.

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45

Ubani, Solomon I. "Cisternae Membrane of Golgi Apparatus." Journal of Progress in Engineering and Physical Science 1, no. 2 (December 2022): 6–9. http://dx.doi.org/10.56397/jpeps.2022.12.02.

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Research was studies of Golgi apparatus an organelle in most eukaryotic cells. The research question was does process RNA constituents of enzymes for the apparatus. Method involved sort of cells production and selection for distribution. A specialized determination indicators known as phosphate were inclusion by enzymes. Results indicated cisterna was a membrane in Golgi apparatus. This consisted three to twenty membranes. This cisternae was between the interior and outside environment. This organelle determined the substances in and out of cells. It can be concluded the covalent attachment to the membrane after its synthesis by A promoter. The cisternae were 15000 to 250000 Daltons in the cellular substances production of the plant.

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46

Keenan, Thomas W. "Biochemistry of the Golgi apparatus." Histochemistry and Cell Biology 109, no. 5-6 (June 5, 1998): 505–16. http://dx.doi.org/10.1007/s004180050251.

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47

Missiaen, Ludwig, Leonard Dode, Jo Vanoevelen, Luc Raeymaekers, and Frank Wuytack. "Calcium in the Golgi apparatus." Cell Calcium 41, no. 5 (May 2007): 405–16. http://dx.doi.org/10.1016/j.ceca.2006.11.001.

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48

Green, SA, and RB Kelly. "Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to the Golgi apparatus at equal rates in PC12 cells." Journal of Cell Biology 117, no. 1 (April 1, 1992): 47–55. http://dx.doi.org/10.1083/jcb.117.1.47.

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Efficient transport of cell surface glycoproteins to the Golgi apparatus has been previously demonstrated for a limited number of proteins, and has been proposed to require selective sorting in the endocytic pathway after internalization. We have studied the endocytic fate of several glycoproteins that accumulate in different organelles in a variant clone of PC12, a regulated secretory cell line. The cation-independent mannose 6-phosphate receptor and the low density lipoprotein receptor, both rapidly internalized from the cell surface, and the synaptic vesicle membrane protein synaptophysin, were transported to the Golgi apparatus with equivalent, nonlinear kinetics. Transport to the Golgi apparatus (t1/2 = 2.5-3.0 h) was several times faster than turnover of these proteins (t1/2 greater than or equal to 20 h), indicating that transport of these proteins to the Golgi apparatus occurred on average several times for each protein. In contrast, Thy-1, a protein anchored in the membrane by a glycosylphosphoinositide group, was internalized and transported to the Golgi apparatus more slowly than the three transmembrane proteins. Since each of the transmembrane proteins studied showed the same t1/2 for transport to the Golgi apparatus, we conclude that transport of these proteins from the cell surface to the Golgi apparatus does not require sorting information specific to any one of these proteins. These results suggest that one of the functions of late endosomes is constitutive recycling of cell surface receptors through the Golgi apparatus if they fail to recycle to the cell surface directly from early endosomes, and that the late endosome recycling pathway is followed frequently by many rapidly internalized proteins.

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49

Munro, Sean. "The Golgi apparatus: defining the identity of Golgi membranes." Current Opinion in Cell Biology 17, no. 4 (August 2005): 395–401. http://dx.doi.org/10.1016/j.ceb.2005.06.013.

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50

Dröscher, Ariane. "Camillo Golgi and the discovery of the Golgi apparatus." Histochemistry and Cell Biology 109, no. 5-6 (June 5, 1998): 425–30. http://dx.doi.org/10.1007/s004180050245.

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