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Phosphorus triiodide (PI 3) is an inorganic compound with the formula PI 3. A red solid, it is too unstable to be stored for long periods of time; it is, nevertheless, commercially available. [ 2 ] It is widely used in organic chemistry for converting alcohols to alkyl iodides and also serves as a powerful reducing agent.
Phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P 3), abbreviated PIP 3, is the product of the class I phosphoinositide 3-kinases' (PI 3-kinases) phosphorylation of phosphatidylinositol (4,5)-bisphosphate (PIP 2). It is a phospholipid that resides on the plasma membrane.
Class II catalyse the production of PI(3)P from PI and PI(3,4)P 2 from PI(4)P; however, little is known about their role in immune cells. PI(3,4)P 2 has, however, been shown to play a role in the invagination phase of clathrin-mediated endocytosis. [17] C2α and C2β are expressed through the body, but expression of C2γ is limited to hepatocytes.
Phosphatidylinositol 3-phosphate (PI3P) is a phospholipid found in cell membranes that helps to recruit a range of proteins, many of which are involved in protein trafficking, to the membranes. It is the product of both the class II and III phosphoinositide 3-kinases (PI 3-kinases) activity on phosphatidylinositol .
Phosphatase and tensin homolog (PTEN) antagonises PI3K by converting PI(3,4,5)P 3 into PI(4,5)P 2. Loss of PTEN function leads to over-activation of Akt and is common in cancer cells (PTEN is a tumour suppressor). SH2-containing Inositol Phosphatase (SHIP) also dephosphorylates PI(3,4,5)P 3, at the 5' position of the inositol ring. [22]
Class III PI 3-kinase is a subgroup of the enzyme family, phosphoinositide 3-kinase that share a common protein domain structure, substrate specificity and method of activation. There is only one known class III PI 3-kinase, Vps34, which is also the only PI 3-kinase expressed in all eukaryotic cells. In humans it is encoded by the PIK3C3 gene.
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[3] [22] PI(3,4)P2 plays another possible role at the PM, promoting cytoskeletal rearrangements through actin regulatory proteins like Lamellipodin. [3] [23] Lamellipodin is recruited to the PM where it is believed to interact with PI(3,4)P2 through its PH domain. Once at the PM, it can regulate lamellipodia actin networks and cell migration by ...