BiP Is a Substrate for src Kinase in Vitro

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 tyrosin...

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Veröffentlicht in:	Biochemical and biophysical research communications 1994-06, Vol.201 (3), p.1548-1553
Hauptverfasser:	Carlino, A., Toledo, H., Vidal, V., Redfield, B., Strassman, J., Abdelghany, M., Racker, E., Weissbach, H., Brot, N.
Format:	Artikel
Sprache:	eng
Schlagworte:	Carrier Proteins - metabolism Chaperonins Heat-Shock Proteins - metabolism In Vitro Techniques Molecular Chaperones Phosphoproteins - metabolism Phosphorylation Phosphotyrosine Proteins Proto-Oncogene Proteins pp60(c-src) - metabolism Recombinant Proteins Tyrosine - analogs & derivatives Tyrosine - metabolism
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Beschreibung
Zusammenfassung:	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.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1994.1880