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PMID: 23086416 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

Molecular analysis of protein-phosphoinositide interactions.

Current topics in microbiology and immunology ·Vol. 362 ·2012-00-00 ·Pages 111-26

Kutateladze TG

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.

MeSH Terms
Animals Cell Membrane/chemistry Humans Phosphatidylinositols/chemistry,physiology Protein Structure, Tertiary Signal Transduction
Chemicals
Phosphatidylinositols
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Kutateladze Tatiana G
Department of Pharmacology, University of Colorado Denver School of Medicine, Aurora, CO 80045, USA. [email protected]
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Article Info
Journal
Current topics in microbiology and immunology
Abbr.
Curr Top Microbiol Immunol
ISSN
0070-217X
Published
2012-00-00
Pages
111-26
Language
English
Region
Germany
NLM ID
0110513
PMCID
PMC3938896
Subset
IM
Grants
NIGMS NIH HHS · R01 GM071424 · United States
NIGMS NIH HHS · GM096863 · United States
NCI NIH HHS · R01 CA113472 · United States
NCI NIH HHS · CA 113472 · United States
NIGMS NIH HHS · R01 GM096863 · United States
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