One lipid, multiple functions: how various pools of PI(4,5)P2 are created in the plasma membrane |
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Authors: | Katarzyna Kwiatkowska |
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Institution: | (1) Laboratory of Plasma Membrane Receptors, Nencki Institute of Experimental Biology, 3 Pasteur St., 02-093 Warsaw, Poland |
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Abstract: | Phosphatidylinositol 4,5-bisphosphate PI(4,5)P2] is a minor lipid of the inner leaflet of the plasma membrane that controls the activity of numerous proteins and serves
as a source of second messengers. This multifunctionality of PI(4,5)P2 relies on mechanisms ensuring transient appearance of PI(4,5)P2 clusters in the plasma membrane. One such mechanism involves phosphorylation of PI(4)P to PI(4,5)P2 by the type I phosphatidylinositol-4-phosphate 5-kinases (PIP5KI) at discrete membrane locations coupled with PI(4)P delivery/synthesis
at the plasma membrane. Simultaneously, both PI(4)P and PI(4,5)P2 participate in anchoring PIP5KI at the plasma membrane via electrostatic bonds. PIP5KI isoforms are also selectively recruited
and activated at the plasma membrane by Rac1, talin, or AP-2 to generate PI(4,5)P2 in ruffles and lamellipodia, focal contacts, and clathrin-coated pits. In addition, PI(4,5)P2 can accumulate at sphingolipid/cholesterol-based rafts following activation of distinct membrane receptors or be sequestered
in a reversible manner due to electrostatic constrains posed by proteins like MARCKS. |
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