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

Clathrin-protein interactions.

Eileen M Lafer1

  • 1Department of Biochemistry, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX, USA. Lafer@UTHSCSA.edu

Traffic (Copenhagen, Denmark)
|July 18, 2002
PubMed
Summary

This review details the complex protein interactions in clathrin-mediated vesicular transport. It integrates structural and biochemical data to explain how clathrin binding partners interact with clathrin.

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

A balance between nucleating and elongating actin filaments controls deformation of protein condensates.

Science advances·2026
Same author

Endocytic accessory proteins assemble clathrin while simultaneously destabilizing protein condensates.

bioRxiv : the preprint server for biology·2026
Same author

Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.

Nature communications·2025
Same author

Epsin1 enforces a condensation-dependent checkpoint for ubiquitylated cargo during clathrin-mediated endocytosis.

Nature communications·2025
Same author

A balance between nucleating and elongating actin filaments controls deformation of protein condensates.

bioRxiv : the preprint server for biology·2025
Same author

Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.

bioRxiv : the preprint server for biology·2025

Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Clathrin-mediated vesicular traffic is crucial for cellular compartmentalization.
  • Significant advancements have been made in determining the 3D structures of clathrin pathway components.
  • Numerous clathrin binding partners have been recently identified and characterized.

Purpose of the Study:

  • To integrate available structural and biochemical data on clathrin interactions.
  • To provide a unified perspective on how clathrin binding partners associate with clathrin.
  • To elucidate the molecular mechanisms underlying clathrin-mediated transport.

Main Methods:

  • Literature review and data integration.
  • Analysis of existing structural data (e.g., X-ray crystallography, cryo-EM).
  • Biochemical assays and interaction studies.

Main Results:

  • Detailed structural insights into clathrin-protein interfaces.
  • Biochemical validation of identified clathrin binding partners.
  • A comprehensive overview of diverse interaction modes between clathrin and its partners.

Conclusions:

  • The structural and biochemical data provide a unified model for clathrin-protein interactions.
  • Understanding these interactions is key to deciphering vesicular transport mechanisms.
  • This review consolidates current knowledge, highlighting future research directions.

Related Experiment Videos