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Papers In Press, published online ahead of print October 5, 2001
Biochemistry, Fukuoka University School of Medicine, Fukuoka, Fukuoka 814-0180
Corresponding Author: yikehara{at}fukuoka-u.ac.jp
We previously demonstrated that the integral membrane protein giantin has the Golgi localization signal at the COOH-terminal cytoplasmic domain (Misumi, Y., Sohda, M., Tashiro, A., Sato, H., and Ikehara, Y. (2001) J. Biol. Chem. 276, 6867-6873). In the present study, using this domain as a bait in the yeast two-hybrid screening system, we identified a novel protein interacting with giantin. The 3.6-kb mRNA encoding a 528-amino-acid protein of 60 kDa (designated as GCP60) was ubiquitously expressed, especially abundant in the testis and ovary. Immunofluorescence and immunoelectron microscopy confirmed that GCP60 was co-localized with giantin in the Golgi complex. GCP60 was found to be a peripheral protein associated with the Golgi membrane, where the COOH-terminal domain of GCP60 interacts with the COOH-terminal cytoplasmic domain of giantin. Overexpression of the COOH-terminal domain of GCP60 caused disassembly of the Golgi structure and blocked protein transport from the endoplasmic reticulum to the Golgi. Taken together, these results suggest that GCP60 is involved in the maintenance of the Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and the Golgi.
J. Biol. Chem, 10.1074/jbc.M108961200
Submitted on September 17, 2001
Revised on October 4, 2001
Accepted on October 5, 2001
Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin
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