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An interaction between zyxin and alpha-actinin.

A W Crawford¹, J W Michelsen, M C Beckerle

¹Department of Biology, University of Utah, Salt Lake City 84112.

The Journal of Cell Biology

|March 1, 1992

Summary

Zyxin, a protein found at cell adhesion sites, directly binds to alpha-actinin, an actin-crosslinking protein. This interaction, confirmed by multiple assays, suggests a role for zyxin and alpha-actinin in coordinating cell structure.

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Area of Science:

Cell Biology
Biochemistry
Cytoskeleton Dynamics

Background:

Zyxin is an 82-kD protein localized to adhesion plaques and stress fiber termini.
It is situated at the cytoplasmic face of the cell membrane's adhesive regions.

Purpose of the Study:

To investigate the interaction between zyxin and the actin-crosslinking protein alpha-actinin.
To characterize the nature and specificity of this interaction.

Main Methods:

Cosedimentation assays with filamentous actin.
Analytical gel filtration to detect protein association in solution.
Blot overlay and solid-phase binding assays to determine binding specificity and affinity.
Double-label immunofluorescence microscopy to assess subcellular colocalization.

Main Results:

Zyxin cosediments with filamentous actin in an alpha-actinin-dependent manner.
Zyxin specifically binds to the N-terminal 27-kD domain of alpha-actinin, which contains the actin-binding site.
A specific, saturable, moderate-affinity interaction between zyxin and alpha-actinin was demonstrated.
Extensive colocalization of zyxin and alpha-actinin was observed in chicken embryo fibroblasts and pigmented retinal epithelial cells.

Conclusions:

Zyxin and alpha-actinin interact specifically and with moderate affinity.
The interaction occurs within the N-terminal actin-binding domain of alpha-actinin.
The significant colocalization supports a biological role for this interaction in membrane-cytoskeletal coordination.

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