title: Phosphoinositide-binding proteins in autophagy.
abstract: Phosphoinositides represent a very small fraction of membrane phospholipids, having fast turnover rates and unique subcellular distributions, which make them perfect for initiating local temporal effects. Seven different phosphoinositide species are generated through reversible phosphorylation of the inositol ring of phosphatidylinositol (PtdIns). The negative charge generated by the phosphates provides specificity for interaction with various protein domains that commonly contain a cluster of basic residues. Examples of domains that bind phosphoinositides include PH domains, WD40 repeats, PX domains, and FYVE domains. Such domains often display specificity toward a certain species or subset of phosphoinositides. Here we will review the current literature of different phosphoinositide-binding proteins involved in autophagy.
authors.affiliation: Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Norway.
authors.forename: Alf Håkon
authors.initials: AH
authors.lastname: Lystad
authors.affiliation: Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Norway.
authors.forename: Anne
authors.initials: A
authors.lastname: Simonsen
mesh_terms: D001343:Autophagy / Q000235:genetics*; D001665:Binding Sites; D010716:Phosphatidylinositols / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding / Q000235:genetics*; D000072417:Protein Domains / Q000235:genetics; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D020449:Repetitive Sequences, Amino Acid / Q000235:genetics
chemical_list: D010716:Phosphatidylinositols; D011506:Proteins
keywords: FYVE; PH; PX; autophagy; phosphoinositide