Premium
Phosphoinositide Signaling in the Control of Membrane Dynamics and Interactions
Author(s) -
De Camilli Pietro
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.90.1
Subject(s) - microbiology and biotechnology , endoplasmic reticulum , second messenger system , membrane contact site , membrane , phosphorylation , cytosol , dephosphorylation , inositol , context (archaeology) , endocytic cycle , chemistry , cell cortex , biology , intracellular , endocytosis , membrane protein , biochemistry , cell , integral membrane protein , receptor , cytoskeleton , phosphatase , paleontology , enzyme
Phosphoinositides, the phosphorylated metabolites of phosphatidyl inositol, are minor components of cell membranes, but play key regulatory roles in cell physiology. The differentially phosphorylated inositol groups of these phospholipids control interactions of the bilayer with cytosolic proteins, regulate intrinsic membrane proteins and function as precursors of intracellular second messengers. As different phosphoinositides are preferentially concentrated on different membranes, they also function as major determinants of membrane identity. The talk will focus on the metabolism of PI4P and PI(4,5)P 2 in the plasma membrane and on the mechanisms that control their dephosphorylation on endocytic membranes. I will also discuss the newly discovered role of these two phosphoinositides in the control of direct contacts between the endoplasmic reticulum (ER) and the plasma membrane. In this context I will focus on contacts mediated by the Extended‐Synaptotagmins (E‐Syts). The E‐Syts are ER‐localized proteins which that mediate PI(4,5)P 2 ‐dependent and Ca 2+ ‐regulated interactions of the ER with the plasma membrane and whose putative function is to mediate glycerophospholipids exchange (but not fusion) between the two membranes (Giordano, Saheki et al. Cell. 153: 1494‐1509, 2013; Schauder et al. Nature. 510: 552‐555, 2014).