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Identification and characterization of a substrate specific for the T cell protein tyrosine kinase ZAP‐70
Author(s) -
Watts J.D.,
Brabb T.,
Bures E.J.,
Wange R.L.,
Samelson L.E.,
Aebersold R.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01241-0
Subject(s) - tyrosine kinase , phosphorylation , substrate (aquarium) , cytoplasm , t cell , microbiology and biotechnology , tyrosine , chemistry , kinase , peptide , protein kinase a , cell , tyrosine phosphorylation , biochemistry , biology , signal transduction , immunology , immune system , ecology
ZAP‐70 is a protein tyrosine kinase (PTK) that plays a critical role in T cell activation. To study the role of ZAP‐70 catalytic activity in this process, a substrate capable of distinguishing between the activities of ZAP‐70 and other PTKs would be useful, especially since it has recently been shown that ZAP‐70 interacts with another T cell PTK, Lck. We have thus identified a site of phosphorylation on the cytoplasmic fragment of the erythrocyte band 3 protein that is recognized by ZAP‐70, but not Lck. A synthetic peptide based on this site has been demonstrated to be a good in vitro substrate for ZAP‐70 and a poor substrate for the T cell PTKs Lck and Itk. This peptide molecule should thus prove useful to many investigators working in the field of T cell activation.