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Literature DB >> 1550958

Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.

Abstract

The endoplasmic reticulum (ER)-localized chaperone protein, GRP78-BiP, is involved in the folding and oligomerization of secreted and membrane proteins, including the simian virus 5 hemagglutinin-neuraminidase (HN) glycoprotein. To understand this interaction better, we have constructed a series of HN mutants in which specific portions of the extracytoplasmic domain have been deleted. Analysis of these mutant polypeptides expressed in CV-1 cells have indicated that GRP78-BiP binds to selective sequences in HN and that there exists more than a single site of interaction. Mutant polypeptides have been characterized that are competent and incompetent for association with GRP78-BiP. These mutants have been used to show that the induction of GRP78-BiP synthesis due to the presence of nonnative protein molecules in the ER is dependent on GRP78-BiP complex formation with its substrates. These studies have implications for the function of the GRP78-BiP protein and the mechanism by which the gene is regulated.

Entities: Gene Species

Mesh：

Substances：

Year: 1992 PMID： 1550958 PMCID： PMC275514 DOI： 10.1091/mbc.3.2.143

Source DB: PubMed Journal: Mol Biol Cell ISSN： 1059-1524 Impact factor: 4.138

56 in total

1. The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature-sensitive and undergoes intracellular aggregation at elevated temperatures.

Authors: R Gibson; S Schlesinger; S Kornfeld
Journal: J Biol Chem Date: 1979-05-10 Impact factor: 5.157

2. Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation.

Authors: J Pouysségur; R P Shiu; I Pastan
Journal: Cell Date: 1977-08 Impact factor: 41.582

3. Complex regulation of heat shock- and glucose-responsive genes in human cells.

Authors: S S Watowich; R I Morimoto
Journal: Mol Cell Biol Date: 1988-01 Impact factor: 4.272

4. Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro.

Authors: C K Kassenbrock; P D Garcia; P Walter; R B Kelly
Journal: Nature Date: 1988-05-05 Impact factor: 49.962

5. Immunoglobulin heavy chain binding protein.

Authors: I G Haas; M Wabl
Journal: Nature Date: 1983 Nov 24-30 Impact factor: 49.962

6. Evidence for a ninth influenza viral polypeptide.

Authors: R A Lamb; P R Etkind; P W Choppin
Journal: Virology Date: 1978-11 Impact factor: 3.616

7. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins.

Authors: Y Kozutsumi; M Segal; K Normington; M J Gething; J Sambrook
Journal: Nature Date: 1988-03-31 Impact factor: 49.962

8. Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene.

Authors: S S Watowich; R I Morimoto; R A Lamb
Journal: J Virol Date: 1991-07 Impact factor: 5.103

9. Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression.

Authors: S C Chang; S K Wooden; T Nakaki; Y K Kim; A Y Lin; L Kung; J W Attenello; A S Lee
Journal: Proc Natl Acad Sci U S A Date: 1987-02 Impact factor: 11.205

10. The mitochondrial chaperonin hsp60 is required for its own assembly.

Authors: M Y Cheng; F U Hartl; A L Horwich
Journal: Nature Date: 1990-11-29 Impact factor: 49.962

21 in total

1. Activation of mammalian unfolded protein response is compatible with the quality control system operating in the endoplasmic reticulum.

Authors: Satomi Nadanaka; Hiderou Yoshida; Fumi Kano; Masayuki Murata; Kazutoshi Mori
Journal: Mol Biol Cell Date: 2004-03-12 Impact factor: 4.138

Analysis in vivo of GRP78-BiP/substrate interactions and their role in induction of the GRP78-BiP gene.

1. The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature-sensitive and undergoes intracellular aggregation at elevated temperatures.

2. Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation.

3. Complex regulation of heat shock- and glucose-responsive genes in human cells.

4. Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro.

5. Immunoglobulin heavy chain binding protein.

6. Evidence for a ninth influenza viral polypeptide.

7. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins.

8. Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene.

9. Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression.

10. The mitochondrial chaperonin hsp60 is required for its own assembly.

1. Activation of mammalian unfolded protein response is compatible with the quality control system operating in the endoplasmic reticulum.

2. Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response.

Review 3. The endoplasmic reticulum and the unfolded protein response.

Review 4. BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum.

Review 5. Endoplasmic reticulum stress sensing in the unfolded protein response.

Review 6. Endoplasmic reticulum stress and the unfolded protein responses in retinal degeneration.

Review 7. Endoplasmic reticulum-mediated unfolded protein response and mitochondrial apoptosis in cancer.

8. Information processing by endoplasmic reticulum stress sensors.

9. Dissociation of glucose-regulated protein Grp78 and Grp78-IgE Fc complexes by ATP.

10. Endoplasmic reticulum stress and inflammation: mechanisms and implications in diabetic retinopathy.