ERP61 IS GRP58, A STRESS-INDUCIBLE LUMINAL ENDOPLASMIC-RETICULUM PROTEIN, BUT IS DEVOID OF PHOSPHATIDYLINOSITIDE-SPECIFIC PHOSPHOLIPASE-C ACTIVITY

被引:67
作者
MAZZARELLA, RA
MARCUS, N
HAUGEJORDEN, SM
BALCAREK, JM
BALDASSARE, JJ
ROY, B
LI, LJ
LEE, AS
GREEN, M
机构
[1] ST LOUIS UNIV,SCH MED,DEPT MICROBIOL,ST LOUIS,MO 63104
[2] ST LOUIS UNIV,SCH MED,DEPT INTERNAL MED,ST LOUIS,MO 63104
[3] SMITHKLINE BEECHAM CLIN LABS,DEPT MOLEC PHARMACOL,KING OF PRUSSIA,PA 19406
[4] UNIV SO CALIF,SCH MED,NORRIS CANC RES INST,DEPT BIOCHEM,LOS ANGELES,CA 90033
关键词
D O I
10.1006/abbi.1994.1064
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Using antibody raised against putative Form I phosphatidylinositide-specific phospholipase C (PI-PLC) and direct amino acid sequencing of the protein recognized by this antibody, we have shown that the antibody reacts with luminal endoplasmic reticulum (ER) proteins, including ERp61. ERp61 possesses a COOH-terminal QEDL sequence that acts as an ER retention signal. Additional experiments have shown, however, that PI-PLC activity is separable from ERp61 and that rat or murine ERp61 expressed in COS cells failed to produce an increase in PI-PLC activity in the COS cells. Finally, we have identified ERp61 as GRP58, a 58-kDa protein inducible by glycosylation block and treatment with the Ca2+ ionophore, A23187. (C) 1994 Academic Press, Inc.
引用
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页码:454 / 460
页数:7
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