GSBS Student Publications

Title

Structural basis for endosomal targeting by FYVE domains

GSBS Program

Biochemistry & Molecular Pharmacology

Publication Date

2003-11-05

UMMS Affiliation

Program in Molecular Medicine; Department of Physiology; Department of Biochemistry and Molecular Pharmacology

Document Type

Article

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The FYVE domain is a conserved protein motif characterized by its ability to bind with high affinity and specificity to phosphatidylinositol 3-phosphate (PI3P), a phosphoinositide highly enriched in early endosomes. The PI3P polar head group contacts specific amino acid residues that are conserved among FYVE domains. Despite full conservation of these residues, the ability of different FYVE domains to bind to endosomes in cells is highly variable. Here we show that the endosomal localization in intact cells absolutely requires structural features intrinsic to the FYVE domain in addition to the PI3P binding pocket. These features are involved in FYVE domain dimerization and in interaction with the membrane bilayer. These interactions, which are determined by non-conserved residues, are likely to be essential for the temporal and spatial control of protein associations at the membrane-cytosol interface within the endocytic pathway.

DOI of Published Version

10.1074/jbc.M310503200

Source

J Biol Chem. 2004 Feb 13;279(7):5958-66. Epub 2003 Oct 31. Link to article on publisher's site

Journal/Book/Conference Title

The Journal of biological chemistry

Related Resources

Link to article in PubMed

PubMed ID

14594806

Share

COinS