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GRIP and coiled-coil domain containing 2

The protein encoded by this gene is a peripheral membrane protein localized to the trans-Golgi network. It is sensitive to brefeldin A. This encoded protein contains a GRIP domain which is thought to be used in targeting. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2009] (from NCBI)
Top mentioned proteins: golgin-97, Rab6, ARF3, TGN38, Rab5
Papers on GCC185
PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity.
Kaibuchi et al., Nagoya, Japan. In Mol Biol Cell, Mar 2015
CLASP2 is known to localize to the TGN through its interaction with the TGN protein GCC185.
Protein flexibility is required for vesicle tethering at the Golgi.
Pfeffer et al., Stanford, United States. In Elife, 2014
GCC185 is a trans Golgi-associated protein that captures vesicles inbound from late endosomes.
Molecular and cellular characterization of GCC185: a tethering protein of the trans-Golgi network.
Pfeffer et al., Stanford, United States. In Methods Mol Biol, 2014
Here, we describe the expression and purification of GCC185, a trans-Golgi-localized, 190-kDa coiled-coil tethering protein.
The Arf family G protein Arl1 is required for secretory granule biogenesis in Drosophila.
Munro et al., Cambridge, United Kingdom. In J Cell Sci, 2014
The gene is essential, and examination of clones of cells lacking Arl1 shows that it is required for recruitment of three of the four GRIP domain golgins to the Golgi, with Drosophila GCC185 being less dependent on Arl1.
ARL4A acts with GCC185 to modulate Golgi complex organization.
Lee et al., Taipei, Taiwan. In J Cell Sci, 2012
Deletion of the ARL4A-interacting region of GCC185 results in inability to maintain Golgi structure and modulate endosome-to-Golgi transport.
GCC185 plays independent roles in Golgi structure maintenance and AP-1-mediated vesicle tethering.
Pfeffer et al., Stanford, United States. In J Cell Biol, 2011
Two distinct domains of GCC185 are needed either for Golgi structure maintenance or transport vesicle tethering. The domain needed for vesicle tethering binds to the clathrin adaptor AP-1.
Rab9-dependent retrograde transport and endosomal sorting of the endopeptidase furin.
Gleeson et al., Melbourne, Australia. In J Cell Sci, 2011
The GTPase Rab9 and the TGN golgin GCC185, components of the late endosome-to-TGN pathway, were required for efficient TGN retrieval of furin.
Identification of different itineraries and retromer components for endosome-to-Golgi transport of TGN38 and Shiga toxin.
Gleeson et al., Melbourne, Australia. In Eur J Cell Biol, 2010
We have previously shown that the retrograde transport of the two model cargos, TGN38 and Shiga toxin, differs in the requirement for TGN golgins; transport of TGN38 requires the TGN golgin GCC88 whereas that of Shiga toxin requires GCC185.
Structural aspects of Rab6-effector complexes.
Khan et al., Dublin, Ireland. In Biochem Soc Trans, 2009
In addition, the structure of Rab6 with the golgin, GCC185, has also been determined.
The localization of the Golgin GCC185 is independent of Rab6A/A' and Arl1.
Gleeson et al., Melbourne, Australia. In Cell, 2009
Study demonstrates that Golgi recruitment of endogenous GCC185 does not involve Rab6A/A' and Arl1.
Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain.
Khan et al., Dublin, Ireland. In Structure, 2009
Comparisons with the recent structure of Rab6 in complex with an unrelated effector, human golgin GCC185, reveals significant conformational changes in the conserved hydrophobic triad of Rab6.
Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi.
Pfeffer et al., Stanford, United States. In Mol Biol Cell, 2009
Results show that GCC185 contains at least six binding sites for as many as 14 different Rab GTPases across its entire length.
Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185.
Pfeffer et al., Stanford, United States. In Cell, 2008
Rab and Arl GTPase family members cooperate in the localization of GCC2.
A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells.
Pfeffer et al., Stanford, United States. In J Cell Biol, 2008
This process requires Rab9 guanosine triphosphatase (GTPase) and the putative tether GCC185.
The golgin GCC88 is required for efficient retrograde transport of cargo from the early endosomes to the trans-Golgi network.
Gleeson et al., Melbourne, Australia. In Mol Biol Cell, 2007
Of the four TGN golgins, p230/golgin-245, golgin-97, GCC185, and GCC88, we show that GCC88 defines a retrograde transport pathway from early endosomes to the TGN.
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