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Dual-mode Imaging of Cutaneous Tissue Oxygenation and Vascular Function

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Distinct Binding Modes of Vinculin Isoforms Underlie Their Functional Differences.

Andrey Krokhotin¹, Muzaddid Sarker², Ernesto Alva Sevilla³

¹Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Departments of Pathology, Genetics and Developmental Biology, Howard Hughes Medical Institute, Stanford Medical School, Palo Alto, CA 94305, USA.

Structure (London, England : 1993)

|August 20, 2019

Summary

Vinculin and metavinculin interact with actin filaments, but metavinculin

Keywords:

actin cardiomyopathy heart metavinculin molecular dynamics vinculin

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Area of Science:

Cell biology
Biochemistry
Biophysics

Background:

Vinculin and metavinculin are crucial for cell structure and movement.
Vinculin can bundle filamentous actin (F-actin), while metavinculin cannot.
Understanding this difference is key to cellular mechanics.

Purpose of the Study:

To investigate the molecular basis for the distinct F-actin bundling activities of vinculin and metavinculin.
To elucidate the structural features responsible for metavinculin's inability to bundle F-actin.

Main Methods:

Computational modeling to analyze protein structures.
Experimental techniques including deletion and point mutagenesis.
Analysis of protein interactions with filamentous actin.

Main Results:

Both vinculin and metavinculin C-termini bind to F-actin.
Metavinculin's tail (MVt) domain has a unique 68 amino acid insert forming a globular subdomain with helix 1 (H1).
This protruding MVt H1 subdomain sterically hinders F-actin bundling.

Conclusions:

The protruding MVt H1 subdomain in metavinculin prevents actin bundling by blocking filament access.
Mutations disrupting the MVt H1 structure restore F-actin bundling activity, mimicking vinculin.
Structural differences in the tail domains dictate the distinct F-actin bundling functions of vinculin and metavinculin.