Peptidyl-prolyl cis-trans isomerase Pin1, also known as Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Rotamase Pin1 and PIN1, peptidyl-prolyl cis/trans isomerase (PPIase), is a nucleus protein. PIN1 is a peptidyl-prolyl isomerase that can alter the conformation of phosphoproteins and so affect protein function and/or stability. PIN1 regulates a number of proteins important for cell-cycle progression and is presumed to operate as a molecular timer of this important process. PIN1 is an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. PIN1 displays a preference for an acidic residue N-terminal to the isomerized proline bond. Alterations in the level of PIN1 can influence hyperproliferative diseases such as cancer. PIN1 has been implicated in multiple aspects of cell cycle regulation. It has been suggested that PIN1 function is required for both normal mitotic progression and reentry into the cell cycle from quiescence. PIN1 is also a target of several oncogenic pathways and is overexpressed in human breast cancer. Its overexpression can lead to upregulation of cyclin-D1 and transformation of breast epithelial cells in collaboration with the oncogenic pathways. PIN1 plays a pivotal role in breast development and may be a promising new anticancer target. Recent data also implicate Pin1 as playing an important role in immune responses, at least in part by increasing the stability of cytokine mRNAs by influencing the protein complexes to which they bind.
Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (PIP4K2A) is a member of the phosphatidylinositol-4-phosphate 5-kinase family. It contains 1 PIPK domain and is expressed ubiquitously, with high levels in the brain. It catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). It may exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. It may regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation, negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. It also involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size.
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.
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