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Article

Structural basis for endosomal targeting by FYVE domains.

The Journal of biological chemistry - 13 Feb 2004

Hayakawa Akira, Hayes Susan J, Lawe Deirdre C, Sudharshan Eathiraj, Tuft Richard, Fogarty Kevin, Lambright David, Corvera Silvia

Abstract excerpt

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...

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Identifiers

PMID: 14594806
DOI: 10.1074/jbc.M310503200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural basis for endosomal targeting by FYVE domains.PMID 14594806Read ↗

The molecular basis of the differential subcellular localization of FYVE domains.Semantic proximity Read ↗

Phosphatidylinositol 3-phosphate recognition by the FYVE domain.Semantic proximity Read ↗

Membrane insertion of the FYVE domain is modulated by pH.Semantic proximity Read ↗

Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs.Semantic proximity Read ↗

Traffic to the malaria parasite food vacuole: a novel pathway involving a phosphatidylinositol 3-phosphate-binding protein.Semantic proximity Read ↗

Phosphoinositides differentially regulate protrudin localization through the FYVE domain.Semantic proximity Read ↗

Mammalian cell morphology and endocytic membrane homeostasis require enzymatically active phosphoinositide 5-kinase PIKfyve.Semantic proximity Read ↗

Essential role of Ca2+/calmodulin in Early Endosome Antigen-1 localization.Semantic proximity Read ↗

FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes.Semantic proximity Read ↗

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