PKN1 (Serine/threonine-Protein Kinase N1, Protease-Activated Kinase 1, PAK-1, Protein Kinase C-like 1, Protein Kinase C-like PKN, Protein Kinase PKN-alpha, Protein-Kinase C-Related Kinase 1, Serine-threonine Protein Kinase N, PAK1, PKN, PRK1, PRKCL1)

Protein kinase N (PKN) is a fatty acid-activated serine/threonine kinase whose catalytic domain exhibits homology with that of the PKC family. PKN associates with Rho via its amino terminus, is activated in a GTP-dependent manner and phosphorylates the head-rod domain of neurofilament protein. A second protein, rhophilin, exhibits 40% sequence identity with the amino terminal Rho binding domain. The enzymatic activity of rhophilin has not been demonstrated and it is possible that it acts through the recruitment of cytoskeletal components that initiate a kinase signaling cascade. Citron interacts...