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

Journal

PROGRESS IN LIPID RESEARCH
Volume 46, Issue 6, Pages 315-327

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.plipres.2007.06.001

Keywords

FYVE domain; PX domain; phosphoinositide; phosphatidylinositol 3-phosphate; membrane

Funding

  1. NCI NIH HHS [R01 CA113472, R01 CA113472-02, CA 113472] Funding Source: Medline
  2. NIGMS NIH HHS [R01 GM071424, GM 071424, R01 GM071424-02] Funding Source: Medline

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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. (C) 2007 Elsevier Ltd. All rights reserved.

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