Calcium/phospholipid-dependent kinase recognizes sites in microtubule-associated protein 2 which are phosphorylated in living brain and are not accessible to other kinases.

摘要: Microtubule-associated protein 2 (MAP-2) purified after microtubule assembly cycles from bovine brain had been shown to contain about 10 esterified phosphates (mol/mol), which were relatively phosphatase resistant and essentially confined the projection domain contributes visible arms on microtubules. The kinase responsible for phosphorylating these sites not identified. We have approached this question by using a that releases bulk of residues then determining can now add additional corresponding those released. Three kinases chosen because their abundance in and/or proximity Of only Ca/phospholipid-dependent was able recognize previously occupied sites. also found MAP-2 isolated rat without contained more phosphate than recognized, greater 30 mol/mol, suggesting 20 inadvertently released during cycles. All 3 (Ca/phospholipid-dependent, cAMP-dependent, Ca/calmodulin-dependent II) recognized MAP-2.