Inhibition by acidic phospholipids of protein degradation by ER‐60 protease, a novel cysteine protease, of endoplasmic reticulum

FEBS Letters

Kito, Makoto¹  Urade, Reiko¹ 

[1] Research Institute for Food Science, Kyoto University, Uji, Kyoto 611, Japan

关键词: Endoplasmic reticulum;    Cysteine protease;    Phospholipid;    ER-60 protease;    Rat;    ER;    endoplasmic reticulum;    TCR;    T cell antigen receptor;    HMG-CoA;    3-hydroxy-3-methylglutaryl coenzyme A;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    PI;    phosphatidylinositol;    PIP2;    phosphatidylinositol 4;    5-bisphosphate;    PS;    phosphatidylserine;    ALLN;    N-acetyl-leucyl-leucyl-norleucinal;    ALLM;    N-acetyl-leucyl-leucyl-methioninal;    TLCK;    N-tosyl-l-lysyl chloromethyl ketone;    TPCK;    N-tosyl-l-phenylalanyl chloromethyl ketone;    bis-Tris;    bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    EGTA;    ethyleneglycol bis(2-aminoethylether)tetraacetic acid;   

DOI  :  10.1016/0014-5793(92)81415-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A protein (ER60) with sequence similarity to phosphoinositide-specific phospholipase C-α purified from rat liver endoplasmic reticulum (ER) degraded ER resident proteins and is really a protease [(1992) J. Biol. Chem. 265, 15152-15159]. Therefore, ER60 is called ER-60 protease. We now show that negatively charged phospholipids, phosphatidylinositol, phosphatidylinositol 4,5-bisphosphate and phosphatidylserine inhibit ER protein degradation by ER-60 protease. Phosphatidylcholine and phosphatidylethanolamine show no effect on the activity of ER-60 protease. With the use of protease inhibitors, ER-60 protease is shown to be a novel cysteine protease distinct from those of the cylosol and lysosomes.

【 授权许可】

Unknown