Interaction Between Several PH Domains And Protein Kinase C

Pleckstrin homology (PH) domain is a kind of functionally domain containing about 120 amino acids, which exists on many protein molecules that involve in cellular signal transduction. The main function of PH domains is to mediate protein-protein and protein-phospholipid interaction. Up to now, several ligands of PH domain such as phospholipids, GPy, PKC, Ga12 and F-actin have been identified. In our previous study, we confirmed that the PH domain of Btk and Itk can interact with protein kinase C. But the relation of other PH domains with PKC remains to be elucidated. PKC is a family of serine/threonine protein kinase, which play significant roles in numerous cellular responses (including cell differentiation, growth control, tumor progression, apoptosis and etc.) Now PKC has been taken as the network center in many cellular signal transduction pathways.In the present study, the PH domain genes of β-ARK1, GRF/c, IRS-1, PLCγ -2/n, GAP and SOS-1 were cloned by RT-PCR. With prokaryotic expressionand western blot, the binding capacity of five PH domains ( β-ARK1, GRF/c,IRS-1, PLC Y -2/n and Btk ) to PKC was determined and the effects of bindingon PKC activity was examined. Finally, the region of PKC binding to PH...