Cloning and characterization of XXXX -associated protein splicing isoforms.

@entity72502 @entity72503 @entity19 @entity1521 @entity12852 @entity51105 @entity72504 @entity56193
@entity56193 -associated protein (CAP) is an adaptor protein that plays important roles in both signal transduction and cytoskeleton rearrangement. Alternative splicing of the gene @entity72502 results in multiple isoforms of CAP protein. We report here the cloning of 3 new CAP isoforms, @entity72503 , @entity72504 , and CAP4, from @entity19 adipose tissue. RT-PCR analyses reveal that the isoform mRNAs are differentially expressed. @entity72503 , @entity72504 , and CAP4 contain a coiled-coil domain. In addition, CAP4 contains a @entity1521 -rich region, part of which exists in @entity72504 . Coimmunoprecipitation experiments show that CAP4 forms a homodimeric complex. While these new isoforms similarly interact with @entity56193 , they exhibit varied binding specificity toward @entity12852 . In contrast to @entity51105 and @entity72503 , CAP4 does not interact with @entity12852 , and @entity72504 binds with low affinity. Immunofluorescence analysis demonstrates differential subcellular localization of Myc-tagged CAP isoforms in 3T3-L1 adipocytes. These results suggest that these new isoforms of CAP might play different signaling roles.
