Identification and characterization of a substrate specific for the T cell protein tyrosine kinase ZAP‐70

FEBS Letters

Brabb, T.¹  Wange, R.L.²  Bures, E.J.¹  Watts, J.D.¹  Aebersold, R.¹  Samelson, L.E.² 

[1] Department of Molecular Biotechnology, University of Washington, Box 357730, Seattle, WA 98195-7730, USA;Cell Biology and Metabolism Branch, NICHD, NIH, Bethesda, MD 20892, USA

关键词: Tyrosine kinase;    T cell;    Band 3 protein;    ZAP-70;    Lck;    Itk;    PTK;    protein tyrosine kinase;    TCR;    T cell antigen receptor;    ITAM;    immunoreceptor tyrosine-based activation motif;    cfb3;    cytoplasmic fragment of the erythrocyte band 3 protein;    MBP;    myelin basic protein;    Itk-KD-GST;    Itk kinase domain GST fusion protein;    TFA;    trifluoroacetic acid;    ESI-MS;    electrospray ionization mass spectrometry;    EGFR;    epidermal growth factor receptor;   

DOI  :  10.1016/S0014-5793(96)01241-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown