Title
The Linker between SH2 and Kinase Domains Positively Regulates Catalysis of the Tec Family Kinases
Document Type
Article
Publication Version
Published Version
Publication Date
4-2007
Journal or Book Title
Biochemistry
Volume
46
Issue
18
First Page
5455
Last Page
5462
DOI
10.1021/bi602512e
Abstract
Tec family nonreceptor tyrosine kinases are key immunological enzymes that control processes that range from T and B cell development to reorganization of the actin cytoskeleton. The full-length Tec kinases have been resistant to crystallization. This lack of structural data and the paucity of in vitro biochemical data for this kinase family leave a void in our understanding of Tec kinase regulation. In this report we have used interleukin-2 tyrosine kinase (Itk) as a model system to gain insight into the regulatory apparatus of the Tec kinases. Use of a quantitative in vitro kinase assay has uncovered an essential role for the short linker region flanked by the SH2 and kinase domains of Itk in positively regulating Itk catalytic activity. The precise residues that allosterically regulate Itk are conserved among Tec kinases, pointing to the conserved nature of this regulatory mechanism within the family. These findings indicate that Tec kinases are not regulated in the same manner as the Src kinases but rather share some of the regulatory features of Csk instead.
Rights
One-time permission is granted only for the use specified in your request. No additional uses are granted (such as derivative works or other editions). For any other uses, please submit a new request.
Copyright Owner
American Chemical Society
Copyright Date
2007
Language
en
File Format
application/pdf
Recommended Citation
Joseph, Raji E.; Min, Lie; and Andreotti, Amy H., "The Linker between SH2 and Kinase Domains Positively Regulates Catalysis of the Tec Family Kinases" (2007). Biochemistry, Biophysics and Molecular Biology Publications. 17.
https://lib.dr.iastate.edu/bbmb_ag_pubs/17
Comments
Reprinted (adapted) with permission from Biotechnology 46 (2007): 5455, doi:10.1021/bi602512e. Copyright 2007 American Chemical Society.