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 tyrosine residues are phosphorylated. Although there is no evidence for this reaction in vivo, it does provide a very efficient method to label BiP.
Carlino
A
A
Roche Research Center, Roche Institute of Molecular Biology, Nutley, NJ 07110.
Toledo
H
H
Vidal
V
V
Redfield
B
B
Strassman
J
J
Abdel-Ghany
M
M
Racker
E
E
Weissbach
H
H
Brot
N
N
D002352:Carrier Proteins / Q000378:metabolism*; D018833:Chaperonins; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins / Q000378:metabolism; D066298:In Vitro Techniques; D018832:Molecular Chaperones; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D019000:Phosphotyrosine; D011506:Proteins; D016392:Proto-Oncogene Proteins pp60(c-src) / Q000378:metabolism*; D011994:Recombinant Proteins; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism
D002352:Carrier Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010750:Phosphoproteins; D011506:Proteins; D011994:Recombinant Proteins; D019000:Phosphotyrosine; D014443:Tyrosine; D016392:Proto-Oncogene Proteins pp60(c-src); D018833:Chaperonins