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Готові списки джерел за темами / Golgi Apparatu / Статті в журналах

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Статті в журналах з теми "Golgi Apparatu"

Автор: Grafiati

Опубліковано: 10 березня 2023

Оновлено: 14 березня 2023

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1

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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Анотація:

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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2

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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Анотація:

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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3

Añel, Alberto Marcelo Diaz, та Vivek Malhotra. "Correction: PKCη is required for β1γ2/β3γ2- and PKD-mediated transport to the cell surface and the organization of the Golgi apparatu". Journal of Cell Biology 169, № 3 (9 травня 2005): 539–40. http://dx.doi.org/10.1083/jcb.200412089042805c.

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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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Анотація:

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

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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7

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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8

Lu, Lei, Guihua Tai, and Wanjin Hong. "Autoantigen Golgin-97, an Effector of Arl1 GTPase, Participates in Traffic from the Endosome to the Trans-Golgi Network." Molecular Biology of the Cell 15, no. 10 (October 2004): 4426–43. http://dx.doi.org/10.1091/mbc.e03-12-0872.

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The precise cellular function of Arl1 and its effectors, the GRIP domain Golgins, is not resolved, despite our recent understanding that Arl1 regulates the membrane recruitment of these Golgins. In this report, we describe our functional study of Golgin-97. Using a Shiga toxin B fragment (STxB)-based in vitro transport assay, we demonstrated that Golgin-97 plays a role in transport from the endosome to the trans-Golgi network (TGN). The recombinant GRIP domain of Golgin-97 as well as antibodies against Golgin-97 inhibited the transport of STxB in vitro. Membrane-associated Golgin-97, but not its cytosolic pool, was required in the in vitro transport assay. The kinetic characterization of inhibition by anti-Golgin-97 antibody in comparison with anti-Syntaxin 16 antibody established that Golgin-97 acts before Syntaxin 16 in endosome-to-TGN transport. Knock down of Golgin-97 or Arl1 by their respective small interference RNAs (siRNAs) also significantly inhibited the transport of STxB to the Golgi in vivo. In siRNA-treated cells with reduced levels of Arl1, internalized STxB was instead distributed peripherally. Microinjection of Golgin-97 antibody led to the fragmentation of Golgi apparatus and the arrested transport to the Golgi of internalized Cholera toxin B fragment. We suggest that Golgin-97 may function as a tethering molecule in endosome-to-TGN retrograde traffic.

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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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Анотація:

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

Dröscher, A. "From the ”apparato reticolare interno" to ”the Golgi": 100 years of Golgi apparatus research." Virchows Archiv 434, no. 2 (February 5, 1999): 103–7. http://dx.doi.org/10.1007/s004280050312.

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11

Zhou, Zhongwei, Xiaotian Sun, Zhenhua Zou, Litao Sun, Tao Zhang, Shaoshi Guo, Ya Wen, et al. "PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130." Cell Research 20, no. 9 (April 27, 2010): 1023–33. http://dx.doi.org/10.1038/cr.2010.56.

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12

Ceriotti, A., and A. Colman. "Protein transport from endoplasmic reticulum to the Golgi complex can occur during meiotic metaphase in Xenopus oocytes." Journal of Cell Biology 109, no. 4 (October 1, 1989): 1439–44. http://dx.doi.org/10.1083/jcb.109.4.1439.

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Анотація:

We have previously shown that Xenopus oocytes arrested at second meiotic metaphase lost their characteristic multicisternal Golgi apparati and cannot secrete proteins into the surrounding medium. In this paper, we extend these studies to ask whether intracellular transport events affecting the movement of secretory proteins from the endoplasmic reticulum to the Golgi apparatus are also similarly inhibited in such oocytes. Using the acquisition of resistance to endoglycosidase H (endo H) as an assay for movement to the Golgi, we find that within 6 h, up to 66% of the influenza virus membrane protein, hemagglutinin (HA), synthesized from injected synthetic RNA, can move to the Golgi apparati in nonmatured oocytes; indeed after longer periods some correctly folded HA can be detected at the cell surface where it distributes in a nonpolarized fashion. In matured oocytes, up to 49% of the HA becomes endo H resistant in the same 6-h period. We conclude that movement from the endoplasmic reticulum to the Golgi can occur in matured oocytes despite the dramatic fragmentation of the Golgi apparati that we observe to occur on maturation. This observation of residual protein movement during meiotic metaphase contrasts with the situation at mitotic metabphase in cultured mammalian cells where all movement ceases, but resembles that in the budding yeast Saccharomyces cerevisiae where transport is unaffected.

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13

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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14

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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15

Gillingham, Alison K., Andrea C. Pfeifer, and Sean Munro. "CASP, the Alternatively Spliced Product of the Gene Encoding the CCAAT-Displacement Protein Transcription Factor, Is a Golgi Membrane Protein Related to Giantin." Molecular Biology of the Cell 13, no. 11 (November 2002): 3761–74. http://dx.doi.org/10.1091/mbc.e02-06-0349.

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Анотація:

Large coiled-coil proteins are being found in increasing numbers on the membranes of the Golgi apparatus and have been proposed to function in tethering of transport vesicles and in the organization of the Golgi stack. Members of one class of Golgi coiled-coil protein, comprising giantin and golgin-84, are anchored to the bilayer by a single C-terminal transmembrane domain (TMD). In this article, we report the characterization of another mammalian coiled-coil protein, CASP, that was originally identified as an alternatively spliced product of the CUTL1 gene that encodes CCAAT-displacement protein (CDP), the human homologue of the Drosophila homeodomain protein Cut. We find that the Caenorhabditis elegans homologues of CDP and CASP are also generated from a single gene. CASP lacks the DNA binding motifs of CDP and was previously reported to be a nuclear protein. Herein, we show that it is in fact a Golgi protein with a C-terminal TMD and shares with giantin and golgin-84 a conserved histidine in its TMD. However, unlike these proteins, CASP has a homologue in Saccharomyces cerevisiae, which we callCOY1. Deletion of COY1 does not affect viability, but strikingly restores normal growth to cells lacking the Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor Gos1p. The conserved histidine is necessary for Coy1p's activity in cells lacking Gos1p, suggesting that the TMD of these transmembrane Golgi coiled-coil proteins is directly involved in their function.

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16

Popa, Stephanie, Julien Villeneuve, Sarah Stewart, Esther Perez Garcia, Anna Petrunkina Harrison, and Kevin Moreau. "Genome-wide CRISPR screening identifies new regulators of glycoprotein secretion." Wellcome Open Research 4 (August 9, 2019): 119. http://dx.doi.org/10.12688/wellcomeopenres.15232.1.

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Анотація:

Background: The fundamental process of protein secretion from eukaryotic cells has been well described for many years, yet gaps in our understanding of how this process is regulated remain. Methods: With the aim of identifying novel genes involved in the secretion of glycoproteins, we used a screening pipeline consisting of a pooled genome-wide CRISPR screen, followed by secondary siRNA screening of the hits to identify and validate several novel regulators of protein secretion. Results: We present approximately 50 novel genes not previously associated with protein secretion, many of which also had an effect on the structure of the Golgi apparatus. We further studied a small selection of hits to investigate their subcellular localisation. One of these, GPR161, is a novel Golgi-resident protein that we propose maintains Golgi structure via an interaction with golgin A5. Conclusions: This study has identified new factors for protein secretion involved in Golgi homeostasis.

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17

Popa, Stephanie, Julien Villeneuve, Sarah Stewart, Esther Perez Garcia, Anna Petrunkina Harrison, and Kevin Moreau. "Genome-wide CRISPR screening identifies new regulators of glycoprotein secretion." Wellcome Open Research 4 (January 16, 2020): 119. http://dx.doi.org/10.12688/wellcomeopenres.15232.2.

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Анотація:

Background: The fundamental process of protein secretion from eukaryotic cells has been well described for many years, yet gaps in our understanding of how this process is regulated remain. Methods: With the aim of identifying novel genes involved in the secretion of glycoproteins, we used a screening pipeline consisting of a pooled genome-wide CRISPR screen, followed by secondary siRNA screening of the hits to identify and validate several novel regulators of protein secretion. Results: We present approximately 50 novel genes not previously associated with protein secretion, many of which also had an effect on the structure of the Golgi apparatus. We further studied a small selection of hits to investigate their subcellular localisation. One of these, GPR161, is a novel Golgi-resident protein that we propose maintains Golgi structure via an interaction with golgin A5. Conclusions: This study has identified new factors for protein secretion involved in Golgi homeostasis.

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18

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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19

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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20

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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21

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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22

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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23

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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24

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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25

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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Анотація:

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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26

Preisinger, Christian, Benjamin Short, Veerle De Corte, Erik Bruyneel, Alexander Haas, Robert Kopajtich, Jan Gettemans та 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, № 7 (22 березня 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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27

Mahmud, Md Abdullah Al, Maki Noguchi, Ayaka Domon, Yuki Tochigi, Kentaro Katayama, and Hiroetsu Suzuki. "Cellular Expression and Subcellular Localization of Wwox Protein During Testicular Development and Spermatogenesis in Rats." Journal of Histochemistry & Cytochemistry 69, no. 4 (February 10, 2021): 257–70. http://dx.doi.org/10.1369/0022155421991629.

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A well-known putative tumor suppressor WW domain–containing oxidoreductase (Wwox) is highly expressed in hormonally regulated tissues and is considered important for the normal development and function of reproductive organs. In this study, we investigated the cellular and subcellular localization of Wwox in normal testes during postnatal days 0–70 using Western blotting and immunohistochemistry. Wwox is expressed in testes at all ages. Immunohistochemistry showed that fetal-type and adult-type Leydig cells, immature and mature Sertoli cells, and germ cells (from gonocytes to step 17 spermatids) expressed Wwox except peritubular myoid cells, step 18–19 spermatids, and mature sperm. Wwox localized diffusely in the cytoplasm with focal intense signals in all testicular cells. These signals gradually condensed in germ cells with their differentiation and colocalized with giantin for cis-Golgi marker and partially with golgin-97 for trans-Golgi marker. Biochemically, Wwox was detected in isolated Golgi-enriched fractions. But Wwox was undetectable in the nucleus. This subcellular localization pattern of Wwox was also confirmed in single-cell suspension. These findings indicate that Wwox is functional in most cell types of testis and might locate into Golgi apparatus via interaction with Golgi proteins. These unique localizations might be related to the function of Wwox in testicular development and spermatogenesis:

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28

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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Анотація:

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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29

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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Анотація:

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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30

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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Анотація:

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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31

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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32

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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33

Colman, A., E. A. Jones, and J. Heasman. "Meiotic maturation in Xenopus oocytes: a link between the cessation of protein secretion and the polarized disappearance of Golgi apparati." Journal of Cell Biology 101, no. 1 (July 1, 1985): 313–18. http://dx.doi.org/10.1083/jcb.101.1.313.

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We have studied the relationship between the timing of the late meiotic events that occur during progesterone-induced oocyte maturation, and intracellular protein transport. We have monitored the secretion of chick oviduct proteins from Xenopus laevis oocytes microinjected with polyadenylated mRNA and found that chick ovalbumin and lysozyme are not secreted during the second meiotic metaphase, in contrast to the earlier prophase stage. Maturation had no detectable effect on the glycosylation of ovalbumin, whereas it affected the glycosylation of chick ovomucoid. As maturation proceeded, the Golgi apparati disappeared in a polarized fashion, beginning in the vegetal half. This disappearance coincided temporally and spatially with that of the nuclear envelope. We speculate that Golgi apparatus disappearance and the block in secretion are causally related.

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34

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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35

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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36

Koreishi, Mayuko, Thomas J. Gniadek, Sidney Yu, Junko Masuda, Yasuko Honjo, and Ayano Satoh. "The Golgin Tether Giantin Regulates the Secretory Pathway by Controlling Stack Organization within Golgi Apparatus." PLoS ONE 8, no. 3 (March 21, 2013): e59821. http://dx.doi.org/10.1371/journal.pone.0059821.

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37

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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Анотація:

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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38

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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39

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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40

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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41

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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42

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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43

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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44

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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45

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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46

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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47

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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48

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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49

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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50

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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