|Other Names||Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma, PIP5K1-gamma, PtdIns(4)P-5-kinase 1 gamma, Phosphatidylinositol 4-phosphate 5-kinase type I gamma, PIP5KIgamma, PIP5K1C, KIAA0589|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth.|
|Cellular Location||Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junction, focal adhesion. Cell junction, adherens junction. Cell projection, ruffle membrane. Cell projection, phagocytic cup. Cell projection, uropodium. Note=Detected in plasma membrane invaginations. Isoform 3 is detected in intracellular vesicle-like structures|
|Tissue Location||Isoform 1 is strongly expressed in brain and also detected in heart and lung. Isoform 2 is strongly expressed in pancreas and liver and in lesser quantities in brain, heart, lung and kidney. Isoform 3 is detected in large amounts in heart and large intestine, is also present in lung, pancreas and thyroid, and to a lesser extent in brain, stomach and kidney|
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Provided below are standard protocols that you may find useful for product applications.
This locus encodes a type I phosphatidylinositol4-phosphate 5-kinase. The encoded protein catalyzes phosphorylationof phosphatidylinositol 4-phosphate, producing phosphatidylinositol4,5-bisphosphate. This enzyme is found at synapses and has beenfound to play roles in endocytosis and cell migration. Mutations atthis locus have been associated with lethal congenital contracturalsyndrome. Alternatively spliced transcript variants encodingdifferent isoforms have been described.
Gallicchio, M.A., et al. Biochim. Biophys. Acta 1803(8):919-930(2010)Kahlfeldt, N., et al. J. Biol. Chem. 285(4):2734-2749(2010)Akieda-Asai, S., et al. PLoS ONE 5 (7), E11755 (2010) :Sun, Y., et al. Breast Cancer Res. 12 (1), R6 (2010) :Schill, N.J., et al. Biochem. J. 422(3):473-482(2009)
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