ADP-RIBOSYLATION OF THE MOLECULAR CHAPERONE GRP78/BIP

被引：34

作者：

LEDFORD, BE ^{[1
]}

LENO, GH ^{[1
]}

机构：

[1] UNIV MISSISSIPPI,MED CTR,DEPT BIOCHEM,JACKSON,MS 39216

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1994年 / 138卷 / 1-2期

关键词：

BIP/GRP78; ADP-RIBOSYLATION; NUTRIENT STARVATION; HEPATOMA SECRETION;

D O I：

10.1007/BF00928456

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Starvation of mouse hepatoma cells for essential amino acids or glucose results in the ADP-ribosylation of the molecular chaperone BiP/GRP78. Addition of the missing nutrient to the medium reverses the reaction. The signal mediating the response to environmental nutrients involves the translational efficiency. An inhibitor of proteins synthesis, cycloheximide, or reduced temperature, both of which reduce translational efficiency, stimulate the ADP-ribosylation of BiP/GRP78. Inhibition of N-linked glycosylation of proteins results in the overproduction of BiP/GRP78. The over produced protein is not ADP-ribosylated suggesting that this is the functional form of BiP/GRP78. The over produced BiP/GRP78 can, however, be ADP-ribosylated if the cells are starved for an essential amino acid. BiP/GRP78 resides in the lumen of the endoplasmic reticulum where it participates in the assembly of secretory and integral membrane proteins. ADP-ribosylation of BiP/GRP78 during starvation is probably part of a nutritional stress response which conserves limited nutrients by slowing flow through the secretory pathway.

引用

页码：141 / 148

页数：8

共 25 条

[1] RECONSTITUTION OF PROTEIN TRANSLOCATION FROM SOLUBILIZED YEAST MEMBRANES REVEALS TOPOLOGICALLY DISTINCT ROLES FOR BIP AND CYTOSOLIC HSC70 [J].

BRODSKY, JL ;

HAMAMOTO, S ;

FELDHEIM, D ;

SCHEKMAN, R .

JOURNAL OF CELL BIOLOGY, 1993, 120 (01) :95-102

[2] ADP-RIBOSYLATION OF THE MR 83,000 STRESS-INDUCIBLE AND GLUCOSE-REGULATED PROTEIN IN AVIAN AND MAMMALIAN-CELLS - MODULATION BY HEAT-SHOCK AND GLUCOSE STARVATION [J].

CARLSSON, L ;

LAZARIDES, E .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1983, 80 (15) :4664-4668

[3] RAT GENE ENCODING THE 78-KDA GLUCOSE-REGULATED PROTEIN GRP78 - ITS REGULATORY SEQUENCES AND THE EFFECT OF PROTEIN GLYCOSYLATION ON ITS EXPRESSION [J].

CHANG, SC ;

WOODEN, SK ;

NAKAKI, T ;

KIM, YK ;

LIN, AY ;

KUNG, L ;

ATTENELLO, JW ;

LEE, AS .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (03) :680-684

[4] PEPTIDE BINDING AND RELEASE BY PROTEINS IMPLICATED AS CATALYSTS OF PROTEIN ASSEMBLY [J].

FLYNN, GC ;

CHAPPELL, TG ;

ROTHMAN, JE .

SCIENCE, 1989, 245 (4916) :385-390

[5] PEPTIDE-BINDING SPECIFICITY OF THE MOLECULAR CHAPERONE BIP [J].

FLYNN, GC ;

POHL, J ;

FLOCCO, MT ;

ROTHMAN, JE .

NATURE, 1991, 353 (6346) :726-730

[6] INTERCONVERSION OF 3 DIFFERENTIALLY MODIFIED AND ASSEMBLED FORMS OF BIP [J].

FREIDEN, PJ ;

GAUT, JR ;

HENDERSHOT, LM .

EMBO JOURNAL, 1992, 11 (01) :63-70

[7] PROTEIN FOLDING IN THE CELL [J].

GETHING, MJ ;

SAMBROOK, J .

NATURE, 1992, 355 (6355) :33-45

[8] IDENTITY OF THE IMMUNOGLOBULIN HEAVY-CHAIN-BINDING PROTEIN WITH THE 78,000-DALTON GLUCOSE-REGULATED PROTEIN AND THE ROLE OF POSTTRANSLATIONAL MODIFICATIONS IN ITS BINDING FUNCTION [J].

HENDERSHOT, LM ;

TING, J ;

LEE, AS .

MOLECULAR AND CELLULAR BIOLOGY, 1988, 8 (10) :4250-4256

[9] INTERACTION OF HEAVY-CHAIN BINDING-PROTEIN (BIP/GRP78) WITH ADENINE-NUCLEOTIDES [J].

KASSENBROCK, CK ;

KELLY, RB .

EMBO JOURNAL, 1989, 8 (05) :1461-1467

[10] THE PRESENCE OF MALFOLDED PROTEINS IN THE ENDOPLASMIC-RETICULUM SIGNALS THE INDUCTION OF GLUCOSE-REGULATED PROTEINS [J].

KOZUTSUMI, Y ;

SEGAL, M ;

NORMINGTON, K ;

GETHING, MJ ;

SAMBROOK, J .

NATURE, 1988, 332 (6163) :462-464

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