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Structure paper

TitleThe Structural Basis of Actin Organization by Vinculin and Metavinculin.
Journal, issue, pagesJ Mol Biol, Vol. 428, Issue 1, Page 10-25, Year 2016
Publish dateJan 16, 2016
AuthorsLaura Y Kim / Peter M Thompson / Hyunna T Lee / Mihir Pershad / Sharon L Campbell / Gregory M Alushin /
PubMed AbstractVinculin is an essential adhesion protein that links membrane-bound integrin and cadherin receptors through their intracellular binding partners to filamentous actin, facilitating mechanotransduction. ...Vinculin is an essential adhesion protein that links membrane-bound integrin and cadherin receptors through their intracellular binding partners to filamentous actin, facilitating mechanotransduction. Here we present an 8.5-Å-resolution cryo-electron microscopy reconstruction and pseudo-atomic model of the vinculin tail (Vt) domain bound to F-actin. Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the Vt helical bundle to mediate actin bundling. We find that an analogous conformational change also occurs in the H1' helix of the tail domain of metavinculin (MVt) upon actin binding, a muscle-specific splice isoform that suppresses actin bundling by Vt. These data support a model in which metavinculin tunes the actin bundling activity of vinculin in a tissue-specific manner, providing a mechanistic framework for understanding metavinculin mutations associated with hereditary cardiomyopathies.
External linksJ Mol Biol / PubMed:26493222 / PubMed Central
MethodsEM (helical sym.)
Resolution7.6 - 19.2 Å
Structure data

6446

3jbi

EMDB-6446: Cryo-EM reconstruction of the vinculin-actin interface
PDB-3jbi: MDFF model of the vinculin tail domain bound to F-actin
Method: EM (helical sym.) / Resolution: 8.5 Å

6447

3jbk

EMDB-6447, PDB-3jbk:
Cryo-EM reconstruction of the metavinculin-actin interface
Method: EM (helical sym.) / Resolution: 8.2 Å

6448

3jbj

EMDB-6448, PDB-3jbj:
Cryo-EM reconstruction of F-actin
Method: EM (helical sym.) / Resolution: 7.6 Å

EMDB-6449:
Unsharpened cryo-EM reconstruction of the vinculin-actin interface for difference map calculation
Method: EM (helical sym.) / Resolution: 8.5 Å

EMDB-6450:
Unsharpened cryo-EM reconstruction of the Vt-GFP-actin interface for difference map calculation
Method: EM (helical sym.) / Resolution: 19.2 Å

EMDB-6451:
Unsharpened cryo-EM reconstruction of the GFP-E892-Vt-actin interface for difference map calculation
Method: EM (helical sym.) / Resolution: 16.4 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • oryctolagus cuniculus (rabbit)
  • gallus gallus (chicken)
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / cytoskeleton / adhesion / actin / cell migration / mechanosensation / metavinculin / vinculin

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