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J. Biochem. Nov (2000); 128(5):793-801
Identification and characterization of novel isoforms of COP I subunits.
Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K
Institute of Biological Sciences and Gene Experiment Center, University of Tsukuba, Tsukuba Science City, Ibaraki 305-8572, Japan.
Abstract: COP I-coated vesicles are involved in vesicular trafficking in the early secretory pathway. The COP I coat is composed of seven subunits, alpha-, beta-, beta'-, gamma-, delta-, epsilon-, and zeta-COPs. Evidence suggests, however, that there may be isoforms of the COP I subunits. In the present study, we identified homologs of gamma-COP (gamma2-COP; original gamma-COP is referred to as gamma1-COP in this paper) and of zeta-COP (zeta2-COP; original zeta-COP is referred to as zeta1-COP). gamma1- and gamma2-COPs, and zeta1- and zeta2-COPs share 80 and 75%, respectively, of amino acids. mRNAs for gamma2-COP and zeta2-COP are expressed ubiquitously, suggesting their fundamental role in cellular function. Immunofluorescence analysis shows that gamma2-COP and zeta2-COP are colocalized with beta-COP in the paranuclear cis-Golgi region. Yeast two-hybrid analysis indicates that gamma1- and gamma2-COPs can directly, albeit promiscuously, interact with zeta1- and zeta2-COPs. Like gamma1-COP, gamma2-COP can form a complex with beta-COP in vivo. The gamma1-COP-containing and gamma2-COP-containing complexes can similarly interact with the cytoplasmic domain of p23. These results indicate that gamma2-COP and zeta2-COP can form a COP I-like complex in place of gamma1-COP and zeta1-COP, respectively, and suggest that the COP I complex and the COP I-like complex are functionally redundant.
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BioGRID: A General Repository for Interaction Datasets.
Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.