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Originally published In Press as doi:10.1074/jbc.M210387200 on November 20, 2002

J. Biol. Chem., Vol. 278, Issue 6, 4216-4226, February 7, 2003
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GRIP Domain-mediated Targeting of Two New Coiled-coil Proteins, GCC88 and GCC185, to Subcompartments of the trans-Golgi Network*

Michael R. Luke, Lars Kjer-Nielsen, Darren L. BrownDagger , Jennifer L. StowDagger , and Paul A. Gleeson§

From The Russell Grimwade School of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Victoria 3010, Australia and Dagger  Institute for Molecular Bioscience and School of Molecular and Microbial Science, University of Queensland, Brisbane 4072, Queensland, Australia

The GRIP domain is a targeting sequence found in a family of coiled-coil peripheral Golgi proteins. Previously we demonstrated that the GRIP domain of p230/golgin245 is specifically recruited to tubulovesicular structures of the trans-Golgi network (TGN). Here we have characterized two novel Golgi proteins with functional GRIP domains, designated GCC88 and GCC185. GCC88 cDNA encodes a protein of 88 kDa, and GCC185 cDNA encodes a protein of 185 kDa. Both molecules are brefeldin A-sensitive peripheral membrane proteins and are predicted to have extensive coiled-coil regions with the GRIP domain at the C terminus. By immunofluorescence and immunoelectron microscopy GCC88 and GCC185, and the GRIP protein golgin97, are all localized to the TGN of HeLa cells. Overexpression of full-length GCC88 leads to the formation of large electron dense structures that extend from the trans-Golgi. These de novo structures contain GCC88 and co-stain for the TGN markers syntaxin 6 and TGN38 but not for alpha 2,6-sialyltransferase, beta -COP, or cis-Golgi GM130. The formation of these abnormal structures requires the N-terminal domain of GCC88. TGN38, which recycles between the TGN and plasma membrane, was transported into and out of the GCC88 decorated structures. These data introduce two new GRIP domain proteins and implicate a role for GCC88 in the organization of a specific TGN subcompartment involved with membrane transport.

* This work was supported by funding from the Australian Research Council (to P. A. G.) and the Australian National Health and Medical Research Council (to J. L. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF525417.

§ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Victoria 3010, Australia. Tel.: 61-3-8344-5912; Fax: 61-3-9347-7730; E-mail: pgleeson@unimelb.edu.au.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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