An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein

The 78,000-dalton glucose-regulated protein (GRP78) and the immunoglobulin heavy-chain-binding protein (BiP) were shown to be the same protein by NH2-terminal sequence comparison. Immunoprecipitation of GRP78-BiP induced by glucose starvation and a temperature-sensitive mutation in a hamster fibroblast cell line demonstrated the association of GRP78-BiP with other cellular proteins. In both fibroblasts and lymphoid cells, GRP78-BiP was found to label with 32Pi and [3H]adenosine. Phosphoamino acid analysis demonstrated that GRP78-BiP is phosphorylated on serine and threonine residues. Conditions which induce increased production of GRP78-BiP resulted in decreased incorporation of 32Pi and [3H]adenosine into GRP78-BiP. Furthermore, we report here that the phosphorylated form of BiP resides in the endoplasmic reticulum and that BiP which is associated with heavy chains is not phosphorylated or labeled with [3H]adenosine, whereas free BiP is. This suggests that posttranslational modifications may be important in regulating the synthesis and binding of BiP.

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Identification of immunoglobulin heavy chain binding protein as glucose-regulated protein 78 on the basis of amino acid sequence, immunological cross-reactivity, and functional activity

Journal of Cell Science ◽

10.1242/jcs.1989.supplement_11.10 ◽

1989 ◽

Vol 1989 (Supplement 11) ◽

pp. 115-137 ◽

Cited By ~ 30

Author(s):

Y. KOZUTSUMI ◽

K. NORMINGTON ◽

E. PRESS ◽

C. SLAUGHTER ◽

J. SAMBROOK ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Heavy Chain ◽

Functional Activity ◽

Binding Protein ◽

Immunoglobulin Heavy Chain ◽

Cross Reactivity ◽

Glucose Regulated Protein

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Translation of glucose-regulated protein 78/immunoglobulin heavy-chain binding protein mRNA is increased in poliovirus-infected cells at a time when cap-dependent translation of cellular mRNAs is inhibited.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.86.15.5795 ◽

1989 ◽

Vol 86 (15) ◽

pp. 5795-5799 ◽

Cited By ~ 77

Author(s):

P. Sarnow

Keyword(s):

Heavy Chain ◽

Binding Protein ◽

Immunoglobulin Heavy Chain ◽

Cellular Mrnas ◽

Infected Cells ◽

Glucose Regulated Protein

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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.

Molecular and Cellular Biology ◽

10.1128/mcb.8.10.4250 ◽

1988 ◽

Vol 8 (10) ◽

pp. 4250-4256 ◽

Cited By ~ 134

Author(s):

L M Hendershot ◽

J Ting ◽

A S Lee

Keyword(s):

Heavy Chain ◽

Posttranslational Modifications ◽

Binding Protein ◽

Fibroblast Cell ◽

Immunoglobulin Heavy Chain ◽

Lymphoid Cells ◽

Temperature Sensitive ◽

Heavy Chains ◽

Binding Function ◽

Glucose Regulated Protein

The 78,000-dalton glucose-regulated protein (GRP78) and the immunoglobulin heavy-chain-binding protein (BiP) were shown to be the same protein by NH2-terminal sequence comparison. Immunoprecipitation of GRP78-BiP induced by glucose starvation and a temperature-sensitive mutation in a hamster fibroblast cell line demonstrated the association of GRP78-BiP with other cellular proteins. In both fibroblasts and lymphoid cells, GRP78-BiP was found to label with 32Pi and [3H]adenosine. Phosphoamino acid analysis demonstrated that GRP78-BiP is phosphorylated on serine and threonine residues. Conditions which induce increased production of GRP78-BiP resulted in decreased incorporation of 32Pi and [3H]adenosine into GRP78-BiP. Furthermore, we report here that the phosphorylated form of BiP resides in the endoplasmic reticulum and that BiP which is associated with heavy chains is not phosphorylated or labeled with [3H]adenosine, whereas free BiP is. This suggests that posttranslational modifications may be important in regulating the synthesis and binding of BiP.

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