SAM68 is recruited and tyrosine phosphorylated by several receptor systems, and once it is phosphorylated, it functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins.It represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. It also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.
