PKC lambda/iota Proteins

Protein Information

The PKC family of serine/threonine kinases, including PRKCI (PKC iota), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.

Synonyms

2310021H13Rik; AI427505; aPKClambda; aPKC-lambda/iota; atypical protein kinase C-lambda/iota; DXS1179E; hypothetical protein; mKIAA4165; nPKC-iota; Pkci; Pkcl; PKClambda; PRKCI; Prkcl; PRKC-lambda/iota; protein kinase C iota; protein kinase C iota type; protein kinase C, iota; protein kinase C, lambda