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GLG1  -  golgi glycoprotein 1

Bos taurus

 
 
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Disease relevance of GLG1

 

High impact information on GLG1

  • Approximately 80% of secreted and membrane proteins (40% of all proteins) of eukaryotes become covalently linked to sugars in the lumen of the Golgi apparatus, a cellular organelle that is part of the secretory system of all eukaryotes [3].
  • The sugar donors are mostly nucleoside diphosphate sugars (nucleotide sugars) and must be translocated from the cytosol, their site of synthesis, across the Golgi apparatus membrane and into the lumen by specific transporters [3].
  • They are, however, consistent with electron microscope studies of the fat secretion process, which indicate that secretory vesicle membranes, derived from the Golgi apparatus, may provide a large proportion of the fat globule membrane [4].
  • Labeling was undetectable in the rough endoplasmic reticulum, its transitional elements, and smooth-membraned structures close to them, the trans Golgi apparatus, mucin droplets, and the plasma membrane [5].
  • Apomucin immunolabeling was found throughout the endoplasmic reticulum and the intermediate compartment and partially overlapped the region of transferase labeling in the Golgi apparatus as demonstrated by double immunolabeling [5].
 

Biological context of GLG1

  • In this study, we find that Tctex-1, a light chain of cytoplasmic dynein, localizes predominantly to the Golgi apparatus in interphase fibroblasts [6].
  • The present study was undertaken to provide an indepth investigation of the relationship between shear stress, GA/MTOC localization, cell migration and nuclear position [7].
  • In agreement with the proposed involvement of the Golgi apparatus during secretion, secreted NSP4 appears to undergo additional posttranslational modification compared to its cell-associated counterpart and is partially resistant to deglycosylation by endoglycosidase H [8].
  • It is likely that the ability to fragment the Golgi apparatus, as well as other activities, are also related to ilimaquinone's influence on methylation chemistry [9].
  • Fertilization introduces the sperm centrosome that can reorganize Golgi proteins, but neither fertilization nor cytokinesis prior to compaction requires a functional Golgi apparatus [10].
 

Anatomical context of GLG1

 

Associations of GLG1 with chemical compounds

 

Other interactions of GLG1

 

Analytical, diagnostic and therapeutic context of GLG1

References

  1. Identification and characterization of the pseudorabies virus UL3.5 protein, which is involved in virus egress. Fuchs, W., Klupp, B.G., Granzow, H., Rziha, H.J., Mettenleiter, T.C. J. Virol. (1996) [Pubmed]
  2. Synthesis and processing of the bovine enteric coronavirus haemagglutinin protein. Hogue, B.G., Kienzle, T.E., Brian, D.A. J. Gen. Virol. (1989) [Pubmed]
  3. Nucleotide sugar transporters of the Golgi apparatus: from basic science to diseases. Caffaro, C.E., Hirschberg, C.B. Acc. Chem. Res. (2006) [Pubmed]
  4. Enzymic characteristics of fat globule membranes from bovine colostrum and bovine milk. Powell, J.T., Järlfors, U., Brew, K. J. Cell Biol. (1977) [Pubmed]
  5. Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Roth, J., Wang, Y., Eckhardt, A.E., Hill, R.L. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  6. Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity. Tai, A.W., Chuang, J.Z., Sung, C.H. J. Biol. Chem. (1998) [Pubmed]
  7. Effect of shear stress upon localization of the Golgi apparatus and microtubule organizing center in isolated cultured endothelial cells. Coan, D.E., Wechezak, A.R., Viggers, R.F., Sauvage, L.R. J. Cell. Sci. (1993) [Pubmed]
  8. Rotavirus Nonstructural Glycoprotein NSP4 Is Secreted from the Apical Surfaces of Polarized Epithelial Cells. Bugarcic, A., Taylor, J.A. J. Virol. (2006) [Pubmed]
  9. Interactions of (-)-ilimaquinone with methylation enzymes: implications for vesicular-mediated secretion. Radeke, H.S., Digits, C.A., Casaubon, R.L., Snapper, M.L. Chem. Biol. (1999) [Pubmed]
  10. Golgi dynamics during meiosis are distinct from mitosis and are coupled to endoplasmic reticulum dynamics until fertilization. Payne, C., Schatten, G. Dev. Biol. (2003) [Pubmed]
  11. Yeast and mammals utilize similar cytosolic components to drive protein transport through the Golgi complex. Dunphy, W.G., Pfeffer, S.R., Clary, D.O., Wattenberg, B.W., Glick, B.S., Rothman, J.E. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  12. A missense mutation in the bovine SLC35A3 gene, encoding a UDP-N-acetylglucosamine transporter, causes complex vertebral malformation. Thomsen, B., Horn, P., Panitz, F., Bendixen, E., Petersen, A.H., Holm, L.E., Nielsen, V.H., Agerholm, J.S., Arnbjerg, J., Bendixen, C. Genome Res. (2006) [Pubmed]
  13. Effect of dichloromethane diphosphonate on calcium homeostatic mechanisms in pregnant cows. Yarrington, J.T., Capen, C.C., Black, H.E., Re, R., Nagode, L.A., Geho, W.B. Am. J. Pathol. (1977) [Pubmed]
  14. Purification and multimeric structure of bovine N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. Kornfeld, R., Bao, M., Brewer, K., Noll, C., Canfield, W.M. J. Biol. Chem. (1998) [Pubmed]
  15. The bovine papillomavirus oncoprotein E5 retains MHC class I molecules in the Golgi apparatus and prevents their transport to the cell surface. Marchetti, B., Ashrafi, G.H., Tsirimonaki, E., O'Brien, P.M., Campo, M.S. Oncogene (2002) [Pubmed]
  16. Implication of sphingolipid metabolism in the stability of the Golgi apparatus. Fukunaga, T., Nagahama, M., Hatsuzawa, K., Tani, K., Yamamoto, A., Tagaya, M. J. Cell. Sci. (2000) [Pubmed]
  17. The AMF-R tubule is a smooth ilimaquinone-sensitive subdomain of the endoplasmic reticulum. Wang, H.J., Benlimame, N., Nabi, I. J. Cell. Sci. (1997) [Pubmed]
  18. Membranes of mammary gland. X. Adenosine triphosphate dependent calcium accumulation by Golgi apparatus rich fractions from bovine mammary gland. Baumrucker, C.R., Keenan, T.W. Exp. Cell Res. (1975) [Pubmed]
  19. Localized cdc42 activation, detected using a novel assay, mediates microtubule organizing center positioning in endothelial cells in response to fluid shear stress. Tzima, E., Kiosses, W.B., del Pozo, M.A., Schwartz, M.A. J. Biol. Chem. (2003) [Pubmed]
  20. ACTH-regulated expression of vascular endothelial growth factor in the adult bovine adrenal cortex: a possible role in the maintenance of the microvasculature. Gaillard, I., Keramidas, M., Liakos, P., Vilgrain, I., Feige, J.J., Vittet, D. J. Cell. Physiol. (2000) [Pubmed]
  21. Bovine floor plate explants secrete SCO-spondin. Guiñazú, M.F., Richter, H.G., Rodríguez, E.M. Cell Tissue Res. (2002) [Pubmed]
  22. Immunocytochemical localization of Mullerian inhibiting substance in the rough endoplasmic reticulum and Golgi apparatus in Sertoli cells of the neonatal calf testis using a monoclonal antibody. Hayashi, M., Shima, H., Hayashi, K., Trelstad, R.L., Donahoe, P.K. J. Histochem. Cytochem. (1984) [Pubmed]
  23. Immunoreactive prolactin in subcellular fractions from bovine mammary tissue. Malven, P.V., Keenan, T.W. J. Dairy Sci. (1983) [Pubmed]
  24. A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack. Waters, M.G., Clary, D.O., Rothman, J.E. J. Cell Biol. (1992) [Pubmed]
  25. Altered Golgi apparatus in hydrostatically loaded articular cartilage chondrocytes. Parkkinen, J.J., Lammi, M.J., Pelttari, A., Helminen, H.J., Tammi, M., Virtanen, I. Ann. Rheum. Dis. (1993) [Pubmed]
  26. Physiological characterization of influenza virus temperature-sensitive mutants defective in the haemagglutinin gene. Ueda, M., Sugiura, A. J. Gen. Virol. (1984) [Pubmed]
  27. Identification of a novel protein (G210) specific to the Golgi apparatus. Hogue-Angeletti, R., Xu, R.Y., Gonatas, J.O., Stieber, A., Gonatas, N.K. J. Histochem. Cytochem. (1989) [Pubmed]
 
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