Studies of quality control of proteins in the endoplasmic reticulum.

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In order to elucidate molecular mechanisms of the quality control of proteins in the endoplasmic reticulum (ER), a research team was organized. Major research results were :the relationship between hydrophobicity of signal peptides and efficiency of translocation of ER membrane was found (Tagaya), function of PDI as a chaperone was determined and PDI related proteins were cloned in yeast (Kikuchi), involvement of calnexin, Bip and proteasome was found in retention and degradation of mutant secretory proteins (Ikehara), recombinant ER-60 protease was expressed and its active residue and ER retention signal were detemined (Kito, Urade), intracellular localization of microsomal triglyceride transfer protein was determined and its interaction with PDI was observed (Sato), cis element was identified for transcriptional control of Bip by Ssalp (Kohno), supression of expression and transportation of procollagen was shown by HSP47 antisense RNA (Hosokawa), involvement of NLS peptide and casein kinase 2 in phosphorylation of GRP94 was found (Miyata), singal for ER retention of Sec12p was determined and funtion of Rerlp was analyzed (Nakano), increased lysophosphatidylethanolamine upon membrane fusion in the regulated exocytosis was identified (Fukuoka).A reseach meeting was organized and the research results were published (Kito).