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Spatiotemporal control of endocytosis by phosphatidylinositol-3,4-bisphosphate
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Journal Article
Spatiotemporal control of endocytosis by phosphatidylinositol-3,4-bisphosphate
2013
Overview
Phosphoinositides are important regulators of intracellular membrane traffic, and although the role of PI(4,5)P
2
has been well characterised, the function of PI(3,4)P
2
remains unclear; here the formation of PI(3,4)P
2
by the class II phosphatidylinositol-3-kinase C2α enzyme is shown to control clathrin-mediated endocytosis.
Endocytosis control by lipid switch
Phosphoinositides are important regulators of intracellular membrane traffic. Although the role of phosphatidylinositol-4,5-bisphosphate has been well characterized, that of phosphatidylinositol-3,4-bisphosphate (PI(3,4)P
2
) remains unclear. In this study, Volker Haucke and colleagues show that formation of PI(3,4)P
2
by the class II phosphatidylinositol-3-kinase C2α (PI(3)K C2α) enzyme spatiotemporally controls clathrin-mediated endocytosis. These findings present a novel function of PI(3,4)P
2
in membrane traffic.
Phosphoinositides serve crucial roles in cell physiology, ranging from cell signalling to membrane traffic
1
,
2
. Among the seven eukaryotic phosphoinositides the best studied species is phosphatidylinositol-4,5-bisphosphate (PI(4,5)P
2
), which is concentrated at the plasma membrane where, among other functions, it is required for the nucleation of endocytic clathrin-coated pits
3
,
4
,
5
,
6
. No phosphatidylinositol other than PI(4,5)P
2
has been implicated in clathrin-mediated endocytosis, whereas the subsequent endosomal stages of the endocytic pathway are dominated by phosphatidylinositol-3-phosphates(PI(3)P)
7
. How phosphatidylinositol conversion from PI(4,5)P
2
-positive endocytic intermediates to PI(3)P-containing endosomes is achieved is unclear. Here we show that formation of phosphatidylinositol-3,4-bisphosphate (PI(3,4)P
2
) by class II phosphatidylinositol-3-kinase C2α (PI(3)K C2α) spatiotemporally controls clathrin-mediated endocytosis. Depletion of PI(3,4)P
2
or PI(3)K C2α impairs the maturation of late-stage clathrin-coated pits before fission. Timed formation of PI(3,4)P
2
by PI(3)K C2α is required for selective enrichment of the BAR domain protein SNX9 at late-stage endocytic intermediates. These findings provide a mechanistic framework for the role of PI(3,4)P
2
in endocytosis and unravel a novel discrete function of PI(3,4)P
2
in a central cell physiological process.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Animals
/ Class II Phosphatidylinositol 3-Kinases - metabolism
/ Clathrin-Coated Vesicles - metabolism
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ letter
/ Lipids
/ Phosphatidylinositol Phosphates - metabolism
/ Phosphoric Monoester Hydrolases - metabolism
/ Plasma
/ Proteins
/ Rodents
/ Science
