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TULA proteins regulate activity of the protein tyrosine kinase Syk by Rachana Agrawal; Nick Carpino; Alexander Tsygankov is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract TULA belongs to a two‐member family: TULA (STS‐2) is a lymphoid protein, whereas STS‐1/TULA‐2 is expressed ubiquitously. TULA proteins were implicated in the regulation of signaling mediated by protein tyrosine kinases (PTKs). The initial experiments did not fully reveal the molecular mechanism of these effects, but suggested that both TULA proteins act in a similar fashion. It was shown recently that STS‐1/TULA‐2 dephosphorylates PTKs. In this study, we analyzed the effects of TULA proteins on Syk, a PTK playing an important role in lymphoid signaling. First, we have shown that TULA‐2 decreases tyrosine phosphorylation of Syk in vivo and in vitro and that the intact phosphatase domain of TULA‐2 is essential for this effect. We have also shown that TULA‐2 exhibits a certain degree of substrate specificity. Our results also indicate that inactivated TULA‐2 increases tyrosine phosphorylation of Syk in cells co‐transfected to overexpress these proteins, thus acting as a dominant‐negative form that suppresses dephosphorylation of Syk caused by endogenous TULA‐2. Furthermore, we have demonstrated that phosphatase activity of TULA is negligible as compared to that of TULA‐2 a

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Author

Rachana Agrawal; Nick Carpino; Alexander Tsygankov

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)