Disease relevance of Golgi Apparatus

• Exocytic transport from the endoplasmic reticulum (ER) to the Golgi complex has been visualized in living cells using a chimera of the temperature-sensitive glycoprotein of vesicular stomatitis virus and green fluorescent protein (ts-G-GFP[ct]) [1].
• The pathogenesis of Lowe syndrome due to deficiency of a phosphatidylinositol 4,5-bisphosphate 5-phosphatase in the Golgi complex is unknown [2].
• In murine erythroleukemia cells, brefeldin A caused a rapid and extensive disorganization of the entire Golgi complex accompanied by the accumulation of membranes in a part of the ER closely associated with ER transitional elements [3].
• The envelope glycoprotein precursor of retroviruses undergoes proteolytic cleavage in the Golgi complex to yield the mature surface and transmembrane (TM) glycoproteins of the virus [4].
• Transport from the Golgi complex was monitored by measuring the proteolytic cleavage of the Semliki Forest virus p62 glycoprotein into the E2 and E3 polypeptide chains [5].

High impact information on Golgi Apparatus

• However, GMP-PNP vesicles fail to target and fuse with the Golgi complex whereas GTP vesicles are functional [6].
• Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum [7].
• Brefeldin A (BFA) is a fungal metabolite that causes a redistribution of the stacked cisternae of the Golgi complex into the endoplasmic reticulum by inhibiting anterograde transport [8].
• Treatment of most cells with brefeldin A (BFA) leads to the retrieval of the Golgi complex to the endoplasmic reticulum, presumably reflecting an inhibition of cytoplasmic coat protein binding to Golgi membranes [9].
• Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin [10].

Chemical compound and disease context of Golgi Apparatus

• Type-C Niemann-Pick disease: low density lipoprotein uptake is associated with premature cholesterol accumulation in the Golgi complex and excessive cholesterol storage in lysosomes [11].
• To further characterize the association between actin microfilaments and the Golgi complex, we have used the Clostridium botulinum toxins C2 and C3, which specifically inhibit actin polymerization and cause depolymerization of F-actin in intact cells by the ADP ribosylation of G-actin monomers and the Rho small GTP-binding protein, respectively [12].
• Incubation of vesicular stomatitis virus-infected cells with short-chain, cell-permeable ceramide (Cer) analogs decreased the rate of viral glycoprotein transport through the Golgi complex and reduced the number of infectious virions released from cells in a concentration-dependent manner [13].
• Evidence for an intrinsic toxicity of phosphatidylcholine to Sec14p-dependent protein transport from the yeast Golgi complex [14].
• The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum [15].

Biological context of Golgi Apparatus

• Our results show that the function of ARF is not limited to the Golgi apparatus, and indicate that there may be a link between the formation of nuclear vesicles during mitosis and proteins involved in secretion [16].
• The amino acid sequence of CD75 is shown to be identical to that of human alpha 2,6 sialyltransferase, believed to be primarily associated with the Golgi complex [17].
• Emp24p is a type I transmembrane protein that is involved in secretory protein transport from the endoplasmic reticulum (ER) to the Golgi complex [18].
• We show here that mutations in the ypt1 gene disrupt transport of carboxypeptidase Y to the vacuole in vivo and transport of pro-alpha-factor to a site of extensive glycosylation in the Golgi apparatus in vitro [19].
• These results show that optineurin links myosin VI to the Golgi complex and plays a central role in Golgi ribbon formation and exocytosis [20].

Anatomical context of Golgi Apparatus

• These data suggest that Sec4p may function as a "G" protein on the vesicle surface to transduce an intracellular signal needed to regulate transport between the Golgi apparatus and the plasma membrane [21].
• In human vascular smooth muscle cells, p53 activation transiently increased surface Fas (CD95) expression by transport from the Golgi complex [22].
• These probably serve not only to protect the peptide-binding site on MHC class II molecules from endogenous peptides, but also to sort MHC class II molecules from the Golgi complex to endosomes and there to retain the class II polypeptides to allow binding of peptides generated from exogenous antigens [23].
• Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex [24].
• ICA 512 is cleaved at its luminal domain and, following exposure at the cell surface, recycles to the Golgi complex region and is sorted into newly formed secretory granules [25].

Associations of Golgi Apparatus with chemical compounds

• In mature, fully polarized neurons the VSV glycoprotein (a basolateral protein in epithelial MDCK cells) moved from the Golgi complex to the dendritic domain, whereas the hemagglutinin protein of FPV (an apically sorted protein in MDCK cells) was targeted preferentially, but not exclusively, to the axon [26].
• This applies to the Golgi complex, where a direct, central role of the phosphatidylinositol 4,5-bisphosphate precursor phosphatidylinositol 4-phosphate has recently been reported [27].
• Both biochemical and genetic data indicate that regulation of the membrane content of phosphatidic acid, diacylglycerol and phosphoinositides is necessary for protein traffic from the Golgi complex [28].
• Interactions among pathways for phosphatidylcholine metabolism, CTP synthesis and secretion through the Golgi apparatus [29].
• Monensin action on the Golgi complex in perfused rat liver: evidence against bile salt vesicular transport [30].

Gene context of Golgi Apparatus

• Immunochemical analyses indicate that PS1 and PS2 are similar in size and localized to similar intracellular compartments (endoplasmic reticulum and Golgi complex) [31].
• Class I molecules are present in all the cisternae of the Golgi complex of T2, but the ratio of HLA-A and -B locus products in the Golgi area differs significantly from that at the cell surface [32].
• Based on these findings, a genetic screen has been devised to isolate mutations that affect retention of Kex2p in the Golgi complex [33].
• GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex [34].
• Glycosylphosphatidylinositol (GPI)-anchored proteins exit the ER in distinct vesicles from other secretory proteins, and this sorting event requires the Rab GTPase Ypt1p, tethering factors Uso1p, and the conserved oligomeric Golgi complex [35].

Analytical, diagnostic and therapeutic context of Golgi Apparatus

• Treatment of pancreatic acini with 5 microM monensin resulted in the swelling and vacuolization of the Golgi cisternae, and in a corresponding annular staining by the mouse serum as observed by immunofluorescence, suggesting that the antigen recognized is on the Golgi complex cisternal membrane [36].
• We used indirect immunofluorescence, immunoelectron microscopy, and a novel Nycodenz gradient centrifugation procedure for separating the ER, the intermediate compartment, and the Golgi complex [37].
• Kinase activity is not required for Golgi complex targeting, as evident from microscopical and cell fractionation studies with kinase-dead PKC mu found to be exclusively located at intracellular membranes [38].
• Centrifugation of these pellets to equilibrium on sucrose density gradients separated vacuolar and Golgi complex marker enzymes into light and dense fractions, respectively [39].
• Dissection of the Golgi complex. II. Density separation of specific Golgi functions in virally infected cells treated with monensin [40].

References