Platelet-derived growth factor stimulates synthesis of PtdIns(3,4,5)P3 by activating a PtdIns(4,5)P2 3-OH kinase

Article Abstract:

Platelet-derived growth factor (PDGF) initiates synthesis of 3-phosphorylated inositol lipids by using a phosphatidylinositol(4,5)-bisphoshate (3)-hydroxy (PtdIns4,5P2 3-OH) kinase. The previous discovery of a very similar mechanism for the release of neutrophils by the formyl-peptide fMet-Leu-Phe indicates that the main function of both PDGF and formyl-peptide is to trigger synthesis of PtdIns(3,4,5)P3 by activating PtdIns(45)P2-selective 3-OH kinase. These reactions may constitute a cellular signalling system.

Physiological aspects, Cellular signal transduction, Protein kinases, Platelet-derived growth factor, Phosphatidylinositol, Phosphatidylinositols

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FYVE fingers bind PtdIns(3)P

Article Abstract:

The FYVE finger, a double-zinc-binding domain, is a protein structure that binds to the membrane lipid phosphatidylinositol-3-phosphate (PtdIns(3)P) with considerable specificity. The fact that mutations in the FYVE fingers of the yeast proteins Vac1p and Vps27p have a negative impact on their ability to sustain membrane traffic to the vacuole is strong functional evidence that FYVE fingers are vital structural elements in a subset of proteins controlling endocytic/vacuolar membrane traffic.

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A functional PtdIns(3)P-binding motif

Article Abstract:

A RING zinc-finger domain at the carboxy terminus of the early-endosomal antigen EEA1 binds directly and specifically to phosphatidylinositol-3-phosphate (PtdIns(3)P). This provides evidence that proteins containing this motif could be downstream effectors of PI(3)K in yeast and mammalian cells. It appears that the specific interaction between EEA1 and PtdIns(3)P could be vital in the control of endosome fusion.

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