Phosphatidylinositol Transfer Protein α Isoform (PITPNA) is found in the cytoplasm and belongs to the PtdIns transfer protein family. PITPNA is a ubiquitous and highly conserved protein in multicellular eukaryotes that catalyzes the exchange of phospholipids between membranes and participates in cellular phospholipid metabolism, signal transduction and vesicular trafficking in vivo. It is expressed in a wide range of tissues and implicated in phospholipase C signaling and in the production of phosphatidylinositol 3, 4, 5-trisphosphate (PIP3) by phosphoinositide-3-kinase.
Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis.
Phosphorylates a large number of substrates in the cytoplasm and the nucleus.
Protein Kinase C Epsilon type is a member of the serine- and threonine-specific protein kinase family that can be activated by calcium and the second messenger diacylglycerol. Protein Kinase C Epsilon contains these domains: one AGC-kinase C-terminal domain; one C2 domain; one protein kinase domain and two phorbol-ester/DAG-type zinc fingers. Protein Kinase C Epsilon phosphorylate a variety of protein targets and has been identified to participate in diverse cellular signaling pathways. It has many different cellular functions; such as neuron channel activation; apoptosis; cardioprotection from ischemia; heat shock response; as well as insulin exocytosis. Protein Kinase C Epsilon also serves as the receptor for phorbol esters; a class of tumor promoters.
Protein kinase C iota type, also known as Atypical protein kinase C-lambda/iota, aPKC-lambda/iota and PRKCI, is a cytoplasm, membrane and nucleus protein which belongs to theprotein kinase superfamily, AGC Ser/Thr protein kinase family and PKC subfamily. PRKCI contains oneAGC-kinase C-terminal domain, oneOPR domain, onephorbol-ester/DAG-type zinc finger and oneprotein kinase domain. PRKCI is predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. It is highly expressed in non-small cell lung cancers. PRKCI is a calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. It may play a role in the secretory response to nutrients. PRKCI is involved in cell polarization processes and the formation of epithelial tight junctions. It is implicated in the activation of several signaling pathways including Ras, c-Src and NF-kappa-B pathways. PRKCI functions in both pro- and anti-apoptotic pathways. It functions in the RAC1/ERK signaling required for transformed growth. PRKCI plays a role in microtubule dynamics through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). PRKCI might be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion.
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