Structural Mechanism of Endosome Docking by the FYVE Domain
10.1126/science.291.5509.1793
Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.

Bibliography

Kutateladze, T., & Overduin, M. (2001). Structural Mechanism of Endosome Docking by the FYVE Domain. Science, 291(5509), 1793–1796.

Authors 2
  1. Tatiana Kutateladze (first)
  2. Michael Overduin (additional)
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Dates
Type When
Created 23 years, 1 month ago (July 27, 2002, 5:47 a.m.)
Deposited 1 year, 7 months ago (Jan. 13, 2024, 3:59 a.m.)
Indexed 1 month, 1 week ago (July 26, 2025, 5:10 a.m.)
Issued 24 years, 6 months ago (March 2, 2001)
Published 24 years, 6 months ago (March 2, 2001)
Published Print 24 years, 6 months ago (March 2, 2001)
Funders 0

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@article{Kutateladze_2001, title={Structural Mechanism of Endosome Docking by the FYVE Domain}, volume={291}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.291.5509.1793}, DOI={10.1126/science.291.5509.1793}, number={5509}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Kutateladze, Tatiana and Overduin, Michael}, year={2001}, month=mar, pages={1793–1796} }