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

Biochem Biophys Res Commun. 2002 Aug 16;296(2):492-6. doi: 10.1016/s0006-291x(02)00900-2.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Gene Library
  • Golgi Apparatus / chemistry
  • Golgi Apparatus / metabolism*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification*
  • Membrane Proteins / metabolism*
  • Mice
  • Molecular Sequence Data
  • Phylogeny
  • Receptors, AMPA / genetics
  • Receptors, AMPA / metabolism
  • Sequence Alignment
  • Tissue Distribution
  • Two-Hybrid System Techniques
  • Zinc Fingers*

Substances

  • GODZ protein, mouse
  • Membrane Proteins
  • Receptors, AMPA
  • glutamate receptor ionotropic, AMPA 1

Associated data

  • GENBANK/AB088044