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Gene Review

GCC2  -  GRIP and coiled-coil domain containing 2

Homo sapiens

Synonyms: 185 kDa Golgi coiled-coil protein, CLL-associated antigen KW-11, CTCL tumor antigen se1-1, GCC185, GRIP and coiled-coil domain-containing protein 2, ...
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High impact information on GCC2

  • GCC185 does not rely on Rab9 for its TGN localization; depletion of GCC185 slightly alters the Golgi ribbon but does not interfere with Golgi function [1].
  • A Functional Role for the GCC185 Golgin in Mannose 6-Phosphate Receptor Recycling [1].
  • Loss of GCC185 triggers enhanced degradation of mannose 6-phosphate receptors and enhanced secretion of hexosaminidase [1].
  • These data assign a specific pathway to an interesting, TGN-localized protein and suggest that GCC185 may participate in the docking of late endosome-derived, Rab9-bearing transport vesicles at the TGN [1].
  • GCC88 cDNA encodes a protein of 88 kDa, and GCC185 cDNA encodes a protein of 185 kDa [2].

Anatomical context of GCC2


Other interactions of GCC2

  • Overexpression of both full-length GCC185 and GCC88 showed distinct and nonoverlapping structures [3].
  • These GCC185-labelled structures included the TGN resident protein alpha2,6 sialyltransferase and excluded the recycling TGN protein, TGN46 [3].

Analytical, diagnostic and therapeutic context of GCC2

  • Overexpression of full-length GCC185 resulted in the appearance of small punctate structures dispersed in the cytoplasm of transfected cells that were identified as membrane tubular structures by immunoelectron microscopy [3].


  1. A Functional Role for the GCC185 Golgin in Mannose 6-Phosphate Receptor Recycling. Reddy, J.V., Burguete, A.S., Sridevi, K., Ganley, I.G., Nottingham, R.M., Pfeffer, S.R. Mol. Biol. Cell (2006) [Pubmed]
  2. GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. Luke, M.R., Kjer-Nielsen, L., Brown, D.L., Stow, J.L., Gleeson, P.A. J. Biol. Chem. (2003) [Pubmed]
  3. Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN. Derby, M.C., van Vliet, C., Brown, D., Luke, M.R., Lu, L., Hong, W., Stow, J.L., Gleeson, P.A. J. Cell. Sci. (2004) [Pubmed]
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