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Inhibition by acidic phospholipids of protein degradation by ER‐60 protease, a novel cysteine protease, of endoplasmic reticulum
Author(s) -
Urade Reiko,
Kito Makoto
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81415-i
Subject(s) - endoplasmic reticulum , protease , phosphatidylinositol , phosphatidylethanolamine , masp1 , cysteine protease , biochemistry , phosphatidylserine , chemistry , proteases , phosphatidylinositol 4,5 bisphosphate , cytosol , phospholipase c , phosphatidylcholine , serine protease , enzyme , phospholipid , signal transduction , membrane
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.