Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structural basis for endosomal targeting by FYVE domains.

Akira Hayakawa1, Susan J Hayes, Deirdre C Lawe

  • 1Program in Molecular Medicine, University of Massachusetts Medical School, Worcester 01605, USA.

The Journal of Biological Chemistry
|November 5, 2003
PubMed
Summary

FYVE domains bind phosphatidylinositol 3-phosphate (PI3P) on endosomes. Additional structural features, beyond PI3P binding, control FYVE domain localization and dimerization for precise cellular targeting.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Sudden death from non-traumatic right atrial appendage rupture: an autopsy case.

Legal medicine (Tokyo, Japan)·2026
Same author

Growth hormone therapy after hematopoietic cell transplantation in childhood: a nationwide survey and longitudinal cohort study.

Frontiers in endocrinology·2026
Same author

Investigating the Influence of Tranexamic Acid on Adipocyte Differentiation in an In Vitro Model.

Annals of plastic surgery·2026
Same author

Two autopsy cases of superficial siderosis: ultrastructural similarity across traumatic and non-traumatic contexts and forensic uncertainties.

Legal medicine (Tokyo, Japan)·2026
Same author

Endosome maturation is orchestrated by inside-out proton signaling through a Na<sup>+</sup>/H<sup>+</sup> exchanger and pH-dependent Rab GTPase cycling.

Research square·2026
Same author

International expert consensus on metric-based characterization of robot-assisted total laparoscopic hysterectomy (RATLH).

Surgical endoscopy·2025

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • FYVE domains are protein motifs that bind phosphatidylinositol 3-phosphate (PI3P).
  • PI3P is a key phosphoinositide enriched in early endosomes.
  • Conserved residues in FYVE domains mediate PI3P binding, yet endosomal localization varies significantly.

Purpose of the Study:

  • To investigate the structural determinants of FYVE domain endosomal localization beyond PI3P binding.
  • To understand the role of FYVE domain intrinsic features in cellular targeting.

Main Methods:

  • Analysis of FYVE domain structure-function relationships.
  • Investigating FYVE domain dimerization and membrane interactions.
  • Cellular localization studies in intact cells.

Related Experiment Videos

Main Results:

  • Endosomal localization of FYVE domains requires intrinsic structural features beyond the PI3P binding pocket.
  • These features mediate FYVE domain dimerization and interaction with the membrane bilayer.
  • Non-conserved residues are critical for these interactions and localization.

Conclusions:

  • FYVE domain endosomal targeting is regulated by structural elements beyond PI3P binding, including dimerization and membrane interactions.
  • These interactions, influenced by non-conserved residues, are crucial for spatial and temporal control of protein recruitment in the endocytic pathway.