Title : Interactions between protein kinase C and pleckstrin homology domains. Inhibition by phosphatidylinositol 4,5-bisphosphate and phorbol 12-myristate 13-acetate.

Pub. Date : 1997 May 16

PMID : 9148913






2 Functional Relationships(s)
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1 Unlike other tested phospholipids, phosphatidylinositol 4,5-bisphosphate, which binds to several PH domains, competed with PKC for binding to the PH domain apparently because their binding sites on the amino-terminal portion of the PH domains overlap. Phosphatidylinositol 4,5-Diphosphate proline rich transmembrane protein 2 Homo sapiens
2 These results indicate that PKC binding to PH domains involve the beta2-beta3 region of the Btk PH domain and the C1 region of PKC, and agents that interact with either of these regions (i.e. phosphatidylinositol 4,5-bisphosphate binding to the PH domain and PMA binding to the C1 region of PKC) might act to regulate PKC-PH domain binding. Phosphatidylinositol 4,5-Diphosphate proline rich transmembrane protein 2 Homo sapiens