Activation of protein kinase C is a key signal transduction event in mesangial cell dedifferentiation and proliferation, yet little is known about downstream substrates or their roles in normal or diseased states. SSeCKS, a novel protein kinase C substrate originally isolated as a src-suppressed negative mitogenic regulator in fibroblasts, controls actinbased cytoskeletal architecture and scaffolds key signaling kinases such as protein kinase C and protein kinase A. Activation of protein kinase C is a key signal transduction event in mesangial cell dedifferentiation. A role for SSeCKS, a PKA/PKC scaffolding protein, has been implicatedduring the process of spermiogenesis and in the actin-based stellate morphology of mesangial cellsSynonyms: SSeCKS, A-kinase anchor protein 12, AKAP12, src-suppressed C kinase substrate.