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Journal articles on the topic 'Golgi Apparatu'

Author: Grafiati

Published: 10 March 2023

Last updated: 31 July 2025

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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 (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

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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 (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 f

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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 (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. Deple

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4

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 (2005): 539–40. http://dx.doi.org/10.1083/jcb.200412089042805c.

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5

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 (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

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6

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 (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

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7

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 (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 e

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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 (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 i

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9

Liu, Chunyi, Mei Mei, Qiuling Li, et al. "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 (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

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10

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

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11

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

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12

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

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13

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 (1989): 1439–44. http://dx.doi.org/10.1083/jcb.109.4.1439.

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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 pr

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14

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 (2002): 3761–74. http://dx.doi.org/10.1091/mbc.e02-06-0349.

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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 prot

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15

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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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 als

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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 (January 16, 2020): 119. http://dx.doi.org/10.12688/wellcomeopenres.15232.2.

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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 als

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17

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

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18

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

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19

Lu, Yiping, Wei Song, Zhiquan Tang, et al. "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 (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%)

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20

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 (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 spermatid

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21

Preisinger, Christian, Benjamin Short, Veerle De Corte та ін. "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 (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 ki

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22

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

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23

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

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24

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

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25

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

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26

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

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27

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

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28

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

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29

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

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30

Benyair, Ron, Avital Eisenberg-Lerner, and Yifat Merbl. "Maintaining Golgi Homeostasis: A Balancing Act of Two Proteolytic Pathways." Cells 11, no. 5 (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 r

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31

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 (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 effec

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32

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 (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 tha

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33

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 (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 contras

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34

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 (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

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35

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 (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 Go

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36

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 (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 extens

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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 (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) G

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38

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 (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 fo

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39

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 (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 i

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40

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 (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 tr

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41

Sin, Alex T. W., and Rene E. Harrison. "Growth of the Mammalian Golgi Apparatus during Interphase." Molecular and Cellular Biology 36, no. 18 (2016): 2344–59. http://dx.doi.org/10.1128/mcb.00046-16.

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During the cell cycle, genetic materials and organelles are duplicated to ensure that there is sufficient cellular content for daughter cells. While Golgi growth in interphase has been observed in lower eukaryotes, the elaborate ribbon structure of the mammalian Golgi apparatus has made it challenging to monitor. Here we demonstrate the growth of the mammalian Golgi apparatus in its protein content and volume during interphase. Through ultrastructural analyses, physical growth of the Golgi apparatus was revealed to occur by cisternal elongation of the individual Golgi stacks. By examining the

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42

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 (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

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Roghi, C., and V. J. Allan. "Dynamic association of cytoplasmic dynein heavy chain 1a with the Golgi apparatus and intermediate compartment." Journal of Cell Science 112, no. 24 (1999): 4673–85. http://dx.doi.org/10.1242/jcs.112.24.4673.

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Microtubule motors, such as the minus end-directed motor, cytoplasmic dynein, play an important role in maintaining the integrity, intracellular location, and function of the Golgi apparatus, as well as in the translocation of membrane between the endoplasmic reticulum and Golgi apparatus. We have immunolocalised conventional cytoplasmic dynein heavy chain to the Golgi apparatus in cultured vertebrate cells. In addition, we present evidence that cytoplasmic dynein heavy chain cycles constitutively between the endoplasmic reticulum and Golgi apparatus: it colocalises partially with the intermed

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Donaldson, J. G., J. Lippincott-Schwartz, G. S. Bloom, T. E. Kreis, and R. D. Klausner. "Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action." Journal of Cell Biology 111, no. 6 (1990): 2295–306. http://dx.doi.org/10.1083/jcb.111.6.2295.

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Brefeldin A (BFA) has a profound effect on the structure of the Golgi apparatus, causing Golgi proteins to redistribute into the ER minutes after drug treatment. Here we describe the dissociation of a 110-kD cytoplasmically oriented peripheral membrane protein (Allan, V. J., and T. E. Kreis. 1986. J. Cell Biol. 103:2229-2239) from the Golgi apparatus as an early event in BFA action, preceding other morphologic changes. In contrast, other peripheral membrane proteins of the Golgi apparatus were not released but followed Golgi membrane into the ER during BFA treatment. The 110-kD protein remaine

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Miles, Suzanne, Heather McManus, Kimberly E. Forsten, and Brian Storrie. "Evidence that the entire Golgi apparatus cycles in interphase HeLa cells." Journal of Cell Biology 155, no. 4 (2001): 543–56. http://dx.doi.org/10.1083/jcb.200103104.

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We tested whether the entire Golgi apparatus is a dynamic structure in interphase mammalian cells by assessing the response of 12 different Golgi region proteins to an endoplasmic reticulum (ER) exit block. The proteins chosen spanned the Golgi apparatus and included both Golgi glycosyltransferases and putative matrix proteins. Protein exit from ER was blocked either by microinjection of a GTP-restricted Sar1p mutant protein in the presence of a protein synthesis inhibitor, or by plasmid-encoded expression of the same dominant negative Sar1p. All Golgi region proteins examined lost juxtanuclea

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46

Xu, Ying, Sen Takeda, Takao Nakata, Yasuko Noda, Yosuke Tanaka, and Nobutaka Hirokawa. "Role of KIFC3 motor protein in Golgi positioning and integration." Journal of Cell Biology 158, no. 2 (2002): 293–303. http://dx.doi.org/10.1083/jcb.200202058.

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KIFC3, a microtubule (MT) minus end–directed kinesin superfamily protein, is expressed abundantly and is associated with the Golgi apparatus in adrenocortical cells. We report here that disruption of the kifC3 gene induced fragmentation of the Golgi apparatus when cholesterol was depleted. Analysis of the reassembly process of the Golgi apparatus revealed bidirectional movement of the Golgi fragments in both wild-type and kifC3−/− cells. However, we observed a markedly reduced inwardly directed motility of the Golgi fragments in cholesterol-depleted kifC3−/− cells compared with either choleste

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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 (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,

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48

Donaldson, J. G., J. Lippincott-Schwartz, and R. D. Klausner. "Guanine nucleotides modulate the effects of brefeldin A in semipermeable cells: regulation of the association of a 110-kD peripheral membrane protein with the Golgi apparatus." Journal of Cell Biology 112, no. 4 (1991): 579–88. http://dx.doi.org/10.1083/jcb.112.4.579.

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The release of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A (BFA) action, preceding the movement of Golgi membrane into the ER. ATP depletion also causes the reversible redistribution of the 110-kD protein from Golgi membrane into the cytosol, although no Golgi disassembly occurs. To further define the effects of BFA on the association of the 110-kD protein with the Golgi apparatus we have used filter perforation techniques to produce semipermeable cells. All previously observed effects of BFA, including the rapid redistribution of the 110-kD p

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Wong, SH, SH Low, and W. Hong. "The 17-residue transmembrane domain of beta-galactoside alpha 2,6-sialyltransferase is sufficient for Golgi retention." Journal of Cell Biology 117, no. 2 (1992): 245–58. http://dx.doi.org/10.1083/jcb.117.2.245.

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beta-Galactoside alpha 2,6-sialyltransferase (ST) is a type II integral membrane protein of the Golgi apparatus involved in the sialylation of N-linked glycans. A series of experiments has shown that the 17-residue transmembrane domain of ST is sufficient to confer localization to the Golgi apparatus when transferred to the corresponding region of a cell surface type II integral membrane protein. Lectin affinity chromatography of chimeric proteins bearing this 17-residue sequence suggests that these chimeric proteins are localized in the trans-Golgi cisternae and/or trans-Golgi network. Furthe

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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 (2013): e59821. http://dx.doi.org/10.1371/journal.pone.0059821.

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