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 the actin-binding function of missing-in-metastasis.

Sung Haeng Lee1, Frederic Kerff, David Chereau

  • 1Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, Philadelphia, PA 19104, USA.

Structure (London, England : 1993)
|February 13, 2007
PubMed
Summary
This summary is machine-generated.

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

Phylogeny of SK channels and functional characterization of the conserved Phe in the S3-S4 loop.

Biophysical journal·2026
Same author

Consecutive catalytic steps of viral RNA polymerase and exonuclease suggest a way to overcome intrinsic nucleotide analogue resistance.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Impact of remdesivir modifications on human HINT1 binding - A structural and functional study in the remdesivir activation pathway.

Structure (London, England : 1993)·2026
Same author

The RLK7-MPK3/6-LEAFY PETIOLE signaling axis mediates growth inhibition during PIP peptide-induced immunity in Arabidopsis.

Plant communications·2026
Same author

Mechanisms of disassembly at the actin filament pointed and barbed ends.

Science advances·2026
Same author

Mechanisms of CARMIL dimerization, autoinhibition, and capping protein binding.

Science advances·2026

The missing-in-metastasis (MIM) protein

Area of Science:

  • Structural biology
  • Cell biology
  • Biochemistry

Background:

  • The adaptor protein missing-in-metastasis (MIM) plays a role in actin dynamics.
  • MIM possesses distinct actin-binding domains: an N-terminal IRSp53/MIM homology domain (IMD) and a C-terminal WASP-homology domain 2 (WH2).

Purpose of the Study:

  • To elucidate the structural basis of MIM's interaction with actin.
  • To compare the structure and potential function of MIM's IMD with the related BAR domain.
  • To characterize the WH2 domain of MIM and IRSp53.

Main Methods:

  • X-ray crystallography was used to determine the structures of MIM's IMD and its WH2 domain bound to actin.
  • Structural comparisons were made between MIM's IMD and BAR domains.
  • The WH2 domain of IRSp53 was also characterized.

Related Experiment Videos

Main Results:

  • The crystal structure of MIM's IMD revealed a dimer with an antiparallel three-helix bundle fold, related to the BAR domain.
  • MIM's IMD and BAR domains exhibit opposite membrane-binding surface curvatures.
  • MIM's WH2 domain is elongated, interacting with all four actin subdomains, and a similar WH2 domain exists in IRSp53.

Conclusions:

  • MIM's IMD structure provides insights into its potential membrane-binding properties and curvature preferences.
  • The WH2 domains of MIM and IRSp53 likely function as scaffolds for actin binding.