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J Biol Chem, Vol. 273, Issue 21, 13129-13135, May 22, 1998
From the Department of Biological Sciences, Stanford University,
Stanford, California 94305-5020
The SRC homology 2 (SH2) domain protein-tyrosine
phosphatase, Corkscrew (CSW) is required for signaling by receptor
tyrosine kinases, including the Sevenless receptor tyrosine kinase
(SEV), which directs Drosophila R7 photoreceptor cell
development. To investigate the role of the different domains of CSW,
we constructed domain-specific csw mutations and assayed
their effects on CSW function. Our results indicate that CSW SH2 domain
function is essential, but either CSW SH2 domain can fulfill this
requirement. We also found that CSW and activated SEV are associated
in vivo in a manner that does not require either CSW SH2
domain function or tyrosine phosphorylation of SEV. In contrast, the
interaction between CSW and Daughter of Sevenless, a CSW substrate, is
dependent on SH2 domain function. These results suggest that the role
of the CSW SH2 domains during SEV signaling is to bind Daughter of Sevenless rather than activated SEV. We also found that although CSW
protein-tyrosine phosphatase activity is required for full CSW
function, a catalytically inactive CSW is capable of providing partial
function. In addition, we found that deletion of either the CSW
protein- tyrosine phosphatase insert or the entire CSW carboxyl
terminus, which includes a conserved DRK/GRB2 SH2 domain binding
sequence, does not abolish CSW function.
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