title: Molecular analysis of protein-phosphoinositide interactions.
abstract: Diverse biological processes including cell growth and survival require transient association of proteins with cellular membranes. A large number of these proteins are drawn to a bilayer through binding of their modular domains to phosphoinositide (PI) lipids. Seven PI isoforms are found to concentrate in distinct pools of intracellular membranes, and this lipid compartmentalization provides an efficient way for recruiting PI-binding proteins to specific cellular organelles. The atomic-resolution structures and membrane docking mechanisms of a dozen PI effectors have been elucidated in the last decade, offering insight into the molecular basis for regulation of the PI-dependent signaling pathways. In this chapter, I summarize the mechanistic aspects of deciphering the 'PI code' by the most common PI-recognizing domains and discuss similarities and differences in the membrane anchoring mechanisms.
authors.affiliation: Department of Pharmacology, University of Colorado Denver School of Medicine, Aurora, CO 80045, USA. Tatiana.Kutateladze@ucdenver.edu
authors.forename: Tatiana G
authors.initials: TG
authors.lastname: Kutateladze
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry; D006801:Humans; D010716:Phosphatidylinositols / Q000737:chemistry / Q000502:physiology*; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
chemical_list: D010716:Phosphatidylinositols