| Primary Identifier | IPR034669 | Type | Domain |
| Short Name | nPKC_epsilon |
| description | Protein kinases C (PKCs) constitute a family of Ser/Thr kinases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain [, ]. Novel PKCs (nPKCs) comprise delta, epsilon, eta, and theta isoforms, which have tandem C1 domains and a C2 domain that does not bind calcium []. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein [, ]. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumour invasion and metastasis[, ]. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage [, ]. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility [].This entry also includes PKCs from invertebrates, such as Pkc98E from Drosophila, which exhibits sequence identity to PKC-epsilon []. |
