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.

Comments

Reprinted (adapted) with permission from Biotechnology 46 (2007): 5455, doi:10.1021/bi602512e. Copyright 2007 American Chemical Society.

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

Language

en

File Format

application/pdf

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