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PubMed · 7517674

BiP is a substrate for src kinase in vitro.

A Carlino·H Toledo·V Vidal·B Redfield·J Strassman·M Abdel-Ghany·E Racker·H Weissbach·N Brot
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Abstract

In a study to investigate the ability of chaperones to modulate src kinase activity, it was observed that BiP, a member of the HSP70 family found in the endoplasmic reticulum, is an excellent substrate for src kinase in vitro. The reaction requires polylysine and the results suggest that two tyrosine residues are phosphorylated. Although there is no evidence for this reaction in vivo, it does provide a very efficient method to label BiP.

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Carrier ProteinsChaperoninsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsIn Vitro TechniquesMolecular ChaperonesPhosphoproteinsPhosphorylationPhosphotyrosineProteinsProto-Oncogene Proteins pp60(c-src)Recombinant ProteinsTyrosineJournal Article

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A Carlino, H Toledo, V Vidal, B Redfield, J Strassman, M Abdel-Ghany, E Racker, H Weissbach, N Brot. 1994-06-30. BiP is a substrate for src kinase in vitro.. https://doi.org/10.1006/bbrc.1994.1880

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