Mutational analysis of the SRC homology 2 domain protein-tyrosine phosphatase Corkscrew.

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摘要：

The homology 2 () domain protein-tyrosine , Corkscrew (CSW) is required for signaling by receptor tyrosine kinases, including the Sevenless receptor tyrosine kinase (), which directs R7 . To investigate the role of the different domains of CSW, we constructed domain-specific mutations and assayed their effects on CSW function. Our results indicate that CSW domain function is essential, but either CSW domain can fulfill this requirement. We also found that CSW and activated are associated in vivo in a manner that does not require either CSW domain function or tyrosine of . In contrast, the interaction between CSW and Daughter of Sevenless, a CSW substrate, is dependent on domain function. These results suggest that the role of the CSW domains during signaling is to bind Daughter of Sevenless rather than activated . We also found that although CSW protein-tyrosine 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 insert or the entire CSW carboxyl terminus, which includes a conserved DRK/domain sequence, does not abolish CSW function.

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关键词：

Cell Line Animals Drosophila Adaptor Proteins, Signal Transducing Proteins Drosophila Proteins DNA Primers Signal Transduction Mutagenesis Base Sequence