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GOLGA3  -  golgin A3

Homo sapiens

Synonyms: GCP170, Golgi complex-associated protein of 170 kDa, Golgin subfamily A member 3, Golgin-160, MEA-2, ...
 
 
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Disease relevance of GOLGA3

 

High impact information on GOLGA3

 

Biological context of GOLGA3

 

Anatomical context of GOLGA3

  • Golgin-160 and PIST colocalize to Golgi membranes and interact in vivo [8].
  • We demonstrate here that, in addition to its nuclear distribution, caspase-2 is localized to the Golgi complex, where it cleaves golgin-160 at a unique site not susceptible to cleavage by other caspases with very similar tetrapeptide specificities [3].
  • The protein as well as the recently described proteins golgin-95 and golgin-160 (M. J. Fritzler, J. C. Hamel, R. L. Ochs, and E. K. L. Chan, J. Exp. Med. 178:49-62, 1993) may belong to a new group of Golgi proteins with a high content of heptad repeats which may exert functions in scaffold formation or vesicle transport [9].
  • We assessed the sensitivity of cell lines stably expressing wild-type or caspase-resistant golgin-160 to several proapoptotic stimuli [10].
  • Cells expressing a caspase-resistant mutant of golgin-160 were strikingly resistant to apoptosis induced by ligation of death receptors and by drugs that induce endoplasmic reticulum (ER) stress, including brefeldin-A, dithiothreitol, and thapsigargin [10].
 

Associations of GOLGA3 with chemical compounds

  • Similar binding experiments identified a leucine-rich repeat within golgin-160 necessary for interaction with PIST [8].
  • Glutathione S-transferase binding experiments identified an internal region of PIST that includes a coiled-coil domain, which interacts directly with golgin-160 [8].
  • Hydropathy analysis shows that GCP170 contains no NH2-terminal signal sequence nor a hydrophobic domain sufficient for participating in membrane localization [11].
  • GCP170 was dissociated from the Golgi membrane in response to brefeldin A as rapidly as a coat protein complex of non-clathrin-coated vesicles (beta-COP, a subunit of coatomer), but did not co-localize with beta-COP on the Golgi membrane when examined by immunoelectron microscopy [11].
  • When cells were extracted with 1% Triton X-100 under microtubule-stabilizing conditions, GCP170 remained in the cells in association with the Golgi complex [11].
  • Mutation of the cysteine blocked the interaction in vitro and disrupted the ability to retain the golgin-160 fragment at the Golgi in cells [12].
 

Co-localisations of GOLGA3

 

Other interactions of GOLGA3

 

Analytical, diagnostic and therapeutic context of GOLGA3

References

  1. Medullary carcinoma of the thyroid gland. Shapiro, M.J. The American surgeon. (1977) [Pubmed]
  2. Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex. Fritzler, M.J., Hamel, J.C., Ochs, R.L., Chan, E.K. J. Exp. Med. (1993) [Pubmed]
  3. Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. Mancini, M., Machamer, C.E., Roy, S., Nicholson, D.W., Thornberry, N.A., Casciola-Rosen, L.A., Rosen, A. J. Cell Biol. (2000) [Pubmed]
  4. Golgin-160 Is Required for the Golgi Membrane Sorting of the Insulin-responsive Glucose Transporter GLUT4 in Adipocytes. Williams, D., Hicks, S.W., Machamer, C.E., Pessin, J.E. Mol. Biol. Cell (2006) [Pubmed]
  5. GCP60 Preferentially Interacts with a Caspase-generated Golgin-160 Fragment. Sbodio, J.I., Hicks, S.W., Simon, D., Machamer, C.E. J. Biol. Chem. (2006) [Pubmed]
  6. Phosphorylation of golgin-160 by mixed lineage kinase 3. Cha, H., Smith, B.L., Gallo, K., Machamer, C.E., Shapiro, P. J. Cell. Sci. (2004) [Pubmed]
  7. Golgin-160 promotes cell surface expression of the Beta-1 adrenergic receptor. Hicks, S.W., Horn, T.A., McCaffery, J.M., Zuckerman, D.M., Machamer, C.E. Traffic (2006) [Pubmed]
  8. Isoform-specific interaction of golgin-160 with the Golgi-associated protein PIST. Hicks, S.W., Machamer, C.E. J. Biol. Chem. (2005) [Pubmed]
  9. Molecular genetic analyses of a 376-kilodalton Golgi complex membrane protein (giantin). Seelig, H.P., Schranz, P., Schröter, H., Wiemann, C., Griffiths, G., Renz, M. Mol. Cell. Biol. (1994) [Pubmed]
  10. Caspase-resistant Golgin-160 disrupts apoptosis induced by secretory pathway stress and ligation of death receptors. Maag, R.S., Mancini, M., Rosen, A., Machamer, C.E. Mol. Biol. Cell (2005) [Pubmed]
  11. Molecular characterization of GCP170, a 170-kDa protein associated with the cytoplasmic face of the Golgi membrane. Misumi, Y., Sohda, M., Yano, A., Fujiwara, T., Ikehara, Y. J. Biol. Chem. (1997) [Pubmed]
  12. Identification of a redox-sensitive cysteine in GCP60 that regulates its interaction with golgin-160. Sbodio, J.I., Machamer, C.E. J. Biol. Chem. (2007) [Pubmed]
  13. Identification and characterization of GCP16, a novel acylated Golgi protein that interacts with GCP170. Ohta, E., Misumi, Y., Sohda, M., Fujiwara, T., Yano, A., Ikehara, Y. J. Biol. Chem. (2003) [Pubmed]
 
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