passages.id: split_1_test_783_passage
passages.type: progene_text
passages.text: Experiments designed to assess this hypothesis now (a) establish the function , boundaries and identity of critical amino acids of the protein kinase AII ( PKAII ) tethering site of DAKAP200 ; (b) demonstrate that residues 119 - 148 mediate binding with Ca(2+) - calmodulin and F-actin ; (c) show that a polybasic region of DAKAP200 is a substrate for protein kinase C ; (d) reveal that phosphorylation of the polybasic domain regulates affinity for F-actin and Ca(2+) - calmodulin ; and (e) indicate that DAKAP200 is myristoylated and that this modification promotes targeting of DAKAP200 to plasma membrane .