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Gene Review

GORASP1  -  golgi reassembly stacking protein 1, 65kDa

Homo sapiens

Synonyms: FLJ23443, GOLPH5, GRASP65, Golgi peripheral membrane protein p65, Golgi phosphoprotein 5, ...
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High impact information on GORASP1

  • GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution [1].
  • This structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil proteins, the golgins, and other peripheral membrane components such as GRASP55 and GRASP65 [2].
  • GRASP55 is homologous to GRASP65, an N-ethylmaleimide-sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system [3].
  • Golgi reassembly stacking protein 65 (GRASP65), an NEM-sensitive membrane-bound component, is required for the stacking process [4].
  • Deletion or frameshift mutations in the conserved C-terminal domain of Plk greatly diminish its ability to phosphorylate GRASP65 [5].

Biological context of GORASP1


Anatomical context of GORASP1


Associations of GORASP1 with chemical compounds

  • The MEK1 requirement for normal mitotic entry was abrogated if Golgi proteins were dispersed before M phase by treatment of cells with brefeldin A or if GRASP65, which links Golgi stacks into a ribbon network, was depleted [11].
  • Saturation solubilities of several para-substituted acetanilides have been measured at 37 degrees C in aqueous solutions of structurally related polyoxyethylene-polyoxypropylene block copolymers-poloxamers L62, L63, L64, P65 and F68 [12].

Other interactions of GORASP1


  1. 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]
  2. Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. Barr, F.A., Preisinger, C., Kopajtich, R., Körner, R. J. Cell Biol. (2001) [Pubmed]
  3. 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]
  4. A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system. Shorter, J., Warren, G. J. Cell Biol. (1999) [Pubmed]
  5. Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2. Lin, C.Y., Madsen, M.L., Yarm, F.R., Jang, Y.J., Liu, X., Erikson, R.L. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  6. Mapping the functional domains of the Golgi stacking factor GRASP65. Wang, Y., Satoh, A., Warren, G. J. Biol. Chem. (2005) [Pubmed]
  7. The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division. Sütterlin, C., Polishchuk, R., Pecot, M., Malhotra, V. Mol. Biol. Cell (2005) [Pubmed]
  8. Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2. Jesch, S.A., Lewis, T.S., Ahn, N.G., Linstedt, A.D. Mol. Biol. Cell (2001) [Pubmed]
  9. The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment. Marra, P., Maffucci, T., Daniele, T., Tullio, G.D., Ikehara, Y., Chan, E.K., Luini, A., Beznoussenko, G., Mironov, A., De Matteis, M.A. Nat. Cell Biol. (2001) [Pubmed]
  10. Dynamics of Golgi matrix proteins after the blockage of ER to Golgi transport. Yoshimura, S., Yamamoto, A., Misumi, Y., Sohda, M., Barr, F.A., Fujii, G., Shakoori, A., Ohno, H., Mihara, K., Nakamura, N. J. Biochem. (2004) [Pubmed]
  11. Mitogen-activated Protein Kinase Kinase 1-dependent Golgi Unlinking Occurs in G2 Phase and Promotes the G2/M Cell Cycle Transition. Feinstein, T.N., Linstedt, A.D. Mol. Biol. Cell (2007) [Pubmed]
  12. Relationships between poloxamer structure and the solubilization of some para-substituted acetanilides. Collett, J.H., Tobin, E.A. J. Pharm. Pharmacol. (1979) [Pubmed]
  13. Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55. Kuo, A., Zhong, C., Lane, W.S., Derynck, R. EMBO J. (2000) [Pubmed]
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