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Prog Lipid Res. 2007 Nov;46(6):315-27. Epub 2007 Jul 13.

Mechanistic similarities in docking of the FYVE and PX domains to phosphatidylinositol 3-phosphate containing membranes.

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1
Department of Pharmacology, University of Colorado Health Sciences Center, Aurora, CO 80045, USA. Tatiana.Kutateladze@UCHSC.edu

Abstract

Phosphatidylinositol 3-phosphate [PtdIns(3)P], a phospholipid produced by PI 3-kinases in early endosomes and multivesicular bodies, often serves as a marker of endosomal membranes. PtdIns(3)P recruits and activates effector proteins containing the FYVE or PX domain and therefore regulates a variety of biological processes including endo- and exocytosis, membrane trafficking, protein sorting, signal transduction and cytoskeletal rearrangement. Structures and PtdIns(3)P binding modes of several FYVE and PX domains have recently been characterized, unveiling the molecular basis underlying multiple cellular functions of these proteins. Here, structural and functional aspects and current mechanisms of the multivalent membrane anchoring by the FYVE and PX domains are reviewed and compared.

PMID:
17707914
PMCID:
PMC2211451
DOI:
10.1016/j.plipres.2007.06.001
[Indexed for MEDLINE]
Free PMC Article
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