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GOLGA2  -  golgin A2

Homo sapiens

Synonyms: 130 kDa cis-Golgi matrix protein, GM130, GM130 autoantigen, Golgin subfamily A member 2, Golgin-95, ...
 
 
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Disease relevance of GOLGA2

 

High impact information on GOLGA2

  • Mitotic fragmentation of the Golgi apparatus can be largely explained by disruption of the interaction between GM130 and the vesicle-docking protein p115 [3].
  • Here we identify a single serine (Ser-25) in GM130 as the key phosphorylated target and Cdc2 as the responsible kinase [3].
  • MEK1, a component of the MAP kinase signaling pathway recently implicated in mitotic Golgi fragmentation, was not required for GM130 phosphorylation or mitotic fragmentation either in vitro or in vivo [3].
  • Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis [3].
  • GRASP65 is complexed with GM130 and is tightly bound to Golgi membranes, even under mitotic conditions when both are heavily phosphorylated [4].
 

Chemical compound and disease context of GOLGA2

  • Using discontinuous sucrose density gradient fractionation of post-nuclear supernatants, prepared from rat tissues and human glioblastoma cell line U373MG, we have identified discrete membrane-bound fractions of alphaB-crystallin, which co-sediment with the Golgi matrix protein, GM130 [2].
 

Biological context of GOLGA2

 

Anatomical context of GOLGA2

 

Associations of GOLGA2 with chemical compounds

  • In addition, GM130 binding activates these kinases by promoting autophosphorylation of a conserved threonine within the T-loop [8].
  • GM130 was not re-distributed to the ER in the presence of brefeldin A but maintained its overlap with syntaxin5 and a partial overlap with the ER-Golgi intermediate compartment marker, p53 [11].
  • When cells were microinjected with Sar1pWT DNA to reverse a guanosine 5'-diphosphate-restricted Sar1p endoplasmic reticulum-exit block phenotype, GM130 and p27 collected perinuclearly with little to no exit of a cisternal enzyme from the endoplasmic reticulum [12].
  • The toxic and mutagenic effects of the alkylating agents methylnitrosourea (MNU) and methylnitronitrosoguanidine (MNNG) and of the frameshift mutagen, ICR-191 were compared among 3 human diploid lymphoblast lines, MIT-2, WI-L2 and GM 130 [13].
  • The glutathione (GSH) content was shown to increase as cells (GM130, HL60, U937) progressed through the cell cycle [14].
 

Physical interactions of GOLGA2

  • Native GM130 and stably expressed HERG were co-immunoprecipitated from HEK-293 cells using GM130 antibodies [1].
  • PIGEA-14 also interacts with GM130, a protein associated with the Golgi matrix, and may therefore represent one important component of the trafficking machinery for polycystin-2 [15].
  • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner [16].
  • These results question a simple tethering model involving a ternary giantin-p115-GM130 complex and suggest that p115-giantin and p115-GM130 interactions might mediate independent membrane tethering events [17].
 

Other interactions of GOLGA2

  • In this process, p115, another coiled-coil protein, is though to bind to giantin on vesicles and to GM130 on cisternae, thus acting as a tether holding the two together [12] [13] [18].
  • We propose that the cytoplasmic C terminus of HERG participates in the tethering or possibly targeting of HERG-containing vesicles within the Golgi via its interaction with GM130 [1].
  • Interestingly, we also show that Iporin interacts with another rab1 interacting partner, the GM130 protein [19].
  • Features of the cDNA suggested that SY11 was a full-length clone encoding golgin-95 but SY2 and SY10 together encoded a partial sequence of golgin-160 [20].
  • Cryo-electron microscopy revealed that GRASP65, like GM130, is present on the cis-Golgi, while GRASP55 is on the medial-Golgi [21].
 

Analytical, diagnostic and therapeutic context of GOLGA2

References

  1. Interaction with GM130 during HERG ion channel trafficking. Disruption by type 2 congenital long QT syndrome mutations. Human Ether-à-go-go-Related Gene. Roti, E.C., Myers, C.D., Ayers, R.A., Boatman, D.E., Delfosse, S.A., Chan, E.K., Ackerman, M.J., January, C.T., Robertson, G.A. J. Biol. Chem. (2002) [Pubmed]
  2. Small heat shock protein alphaB-crystallin is part of cell cycle-dependent Golgi reorganization. Gangalum, R.K., Schibler, M.J., Bhat, S.P. J. Biol. Chem. (2004) [Pubmed]
  3. Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Lowe, M., Rabouille, C., Nakamura, N., Watson, R., Jackman, M., Jämsä, E., Rahman, D., Pappin, D.J., Warren, G. Cell (1998) [Pubmed]
  4. GRASP65, a protein involved in the stacking of Golgi cisternae. Barr, F.A., Puype, M., Vandekerckhove, J., Warren, G. Cell (1997) [Pubmed]
  5. GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Puthenveedu, M.A., Bachert, C., Puri, S., Lanni, F., Linstedt, A.D. Nat. Cell Biol. (2006) [Pubmed]
  6. Evidence that the entire Golgi apparatus cycles in interphase HeLa cells: sensitivity of Golgi matrix proteins to an ER exit block. Miles, S., McManus, H., Forsten, K.E., Storrie, B. J. Cell Biol. (2001) [Pubmed]
  7. The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130. Lowe, M., Gonatas, N.K., Warren, G. J. Cell Biol. (2000) [Pubmed]
  8. YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta. Preisinger, C., Short, B., De Corte, V., Bruyneel, E., Haas, A., Kopajtich, R., Gettemans, J., Barr, F.A. J. Cell Biol. (2004) [Pubmed]
  9. The BTB-kelch protein LZTR-1 is a novel Golgi protein that is degraded upon induction of apoptosis. Nacak, T.G., Leptien, K., Fellner, D., Augustin, H.G., Kroll, J. J. Biol. Chem. (2006) [Pubmed]
  10. Analogs of the Golgi complex in microsporidia: structure and avesicular mechanisms of function. Beznoussenko, G.V., Dolgikh, V.V., Seliverstova, E.V., Semenov, P.B., Tokarev, Y.S., Trucco, A., Micaroni, M., Di Giandomenico, D., Auinger, P., Senderskiy, I.V., Skarlato, S.O., Snigirevskaya, E.S., Komissarchik, Y.Y., Pavelka, M., De Matteis, M.A., Luini, A., Sokolova, Y.Y., Mironov, A.A. J. Cell. Sci. (2007) [Pubmed]
  11. Characterization of a cis-Golgi matrix protein, GM130. Nakamura, N., Rabouille, C., Watson, R., Nilsson, T., Hui, N., Slusarewicz, P., Kreis, T.E., Warren, G. J. Cell Biol. (1995) [Pubmed]
  12. Dynamic nucleation of Golgi apparatus assembly from the endoplasmic reticulum in interphase hela cells. Kasap, M., Thomas, S., Danaher, E., Holton, V., Jiang, S., Storrie, B. Traffic (2004) [Pubmed]
  13. Comparison of toxicity and mutagenicity of methylnitrosourea, methylnitronitrosoguanidine and ICR-191 among human lymphoblast lines. Slapikoff, S.A., Andon, B.M., Thilly, W.G. Mutat. Res. (1980) [Pubmed]
  14. Simultaneous analysis of relative DNA and glutathione content in viable cells by phase-resolved flow cytometry. Keij, J.F., Bell-Prince, C., Steinkamp, J.A. Cytometry. (1999) [Pubmed]
  15. Polycystin-2--an intracellular or plasma membrane channel? Witzgall, R. Naunyn Schmiedebergs Arch. Pharmacol. (2005) [Pubmed]
  16. The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Nakamura, N., Lowe, M., Levine, T.P., Rabouille, C., Warren, G. Cell (1997) [Pubmed]
  17. Binding relationships of membrane tethering components. The giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus. Linstedt, A.D., Jesch, S.A., Mehta, A., Lee, T.H., Garcia-Mata, R., Nelson, D.S., Sztul, E. J. Biol. Chem. (2000) [Pubmed]
  18. A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Barr, F.A. Curr. Biol. (1999) [Pubmed]
  19. Identification and characterization of Iporin as a novel interaction partner for rab1. Bayer, M., Fischer, J., Kremerskothen, J., Ossendorf, E., Matanis, T., Konczal, M., Weide, T., Barnekow, A. BMC Cell Biol. (2005) [Pubmed]
  20. 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]
  21. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. Shorter, J., Watson, R., Giannakou, M.E., Clarke, M., Warren, G., Barr, F.A. EMBO J. (1999) [Pubmed]
  22. Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER. Valsdottir, R., Hashimoto, H., Ashman, K., Koda, T., Storrie, B., Nilsson, T. FEBS Lett. (2001) [Pubmed]
  23. Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae. Barr, F.A., Nakamura, N., Warren, G. EMBO J. (1998) [Pubmed]
  24. Retention at the cis-Golgi and delayed degradation of tissue-non-specific alkaline phosphatase with an Asn153-->Asp substitution, a cause of perinatal hypophosphatasia. Ito, M., Amizuka, N., Ozawa, H., Oda, K. Biochem. J. (2002) [Pubmed]
 
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