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Biochem Biophys Res Commun. 2002 Aug 16;296(2):492-6.

Isolation and characterization of Golgi apparatus-specific GODZ with the DHHC zinc finger domain.

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Department of Molecular Neurobiology and Pharmacology, Graduate School of Medicine, University of Tokyo, and SORST, Japan Science and Technology Corporation, Hongo 7-3-1, Bunkyo-ku, Tokyo, Japan.


We identified a novel Golgi apparatus-specific protein with the DHHC zinc finger domain and four putative transmembrane regions, designated as GODZ. The amino acid sequences were highly conserved among mouse and human GODZs and homologous proteins in human, mouse, rat, Drosophila melanogaster, and Caenorhabditis elegans, implying a functional significance of the GODZ protein family. Overexpression of mouse GODZ in COS7 cells suppressed the sorting of the glutamate receptor GluRalpha1 from the Golgi apparatus. These results suggest that GODZ plays a role in the membrane protein trafficking.

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