The Localization of the Golgin GCC185 Is Independent of Rab6A/A' and Arl1

• Published in: Cell Vol. 138; no. 4; pp. 787 - 794
• Main Authors: Houghton, Fiona J., Chew, Pau Ling, Lodeho, Sylvain, Goud, Bruno, Gleeson, Paul A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 21.08.2009
• Subjects: ADP-Ribosylation Factors - analysis; ADP-Ribosylation Factors - metabolism; CELLBIO; Cytosol; Golgi Apparatus - chemistry; HeLa Cells; Humans; Membrane Proteins - analysis; Membrane Proteins - metabolism; Protein Transport; PROTEINS; rab GTP-Binding Proteins - analysis; rab GTP-Binding Proteins - metabolism; CELLBIO; PROTEINS
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/j.cell.2009.05.048

Mammalian golgins of the trans-Golgi network (TGN) are small G protein effectors that are required for membrane transport and contain a Golgi targeting C-terminal GRIP domain. The localization of two TGN golgins, p230/golgin-245 and golgin-97, is mediated by the small GTPase Arl1, whereas recruitment of the TGN golgin GCC185 is controversial. Recently, GCC185 was proposed to localize to the Golgi by the co-operation of two small GTPases, Rab6A/A' and Arl1 (Burguete et al., 2008), a model based predominantly on in vitro interactions. Here we demonstrate that Golgi recruitment of endogenous GCC185 does not involve Rab6A/A' and Arl1. We find minimal colocalization between Rab6A/A' and endogenous GCC185 on Golgi membranes and failed to detect an interaction between Rab6A/A' and C-terminal domains of GCC185 by yeast two-hybrid analyses. Moreover, depletion of both Rab6A/A' and Arl1 also had no effect on the localization of endogenous GCC185 or the isolated GRIP domain of GCC185.