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Originally published as MBoC in Press, 10.1091/mbc.E08-06-0584 on March 4, 2009

Vol. 20, Issue 9, 2361-2370, May 1, 2009

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The ALP-Enigma Protein ALP-1 Functions in Actin Filament Organization to Promote Muscle Structural Integrity in Caenorhabditis elegans

Hsiao-Fen Han, and Mary C. Beckerle

University of Utah, Salt Lake City, UT 84112

Submitted June 10, 2008; Revised February 19, 2009; Accepted February 23, 2009
Monitoring Editor: Marianne Bronner-Fraser

Mutations that affect the Z-disk–associated ALP-Enigma proteins have been linked to human muscular and cardiac diseases. Despite their clear physiological significance for human health, the mechanism of action of ALP-Enigma proteins is largely unknown. In Caenorhabditis elegans, the ALP-Enigma protein family is encoded by a single gene, alp-1; thus C. elegans provides an excellent model to study ALP-Enigma function. Here we present a molecular and genetic analysis of ALP-Enigma function in C. elegans. We show that ALP-1 and {alpha}-actinin colocalize at dense bodies where actin filaments are anchored and that the proper localization of ALP-1 at dense bodies is dependent on {alpha}-actinin. Our analysis of alp-1 mutants demonstrates that ALP-1 functions to maintain actin filament organization and participates in muscle stabilization during contraction. Reducing {alpha}-actinin activity enhances the actin filament phenotype of the alp-1 mutants, suggesting that ALP-1 and {alpha}-actinin function in the same cellular process. Like {alpha}-actinin, alp-1 also interacts genetically with a connectin/titin family member, ketn-1, to provide mechanical stability for supporting body wall muscle contraction. Taken together, our data demonstrate that ALP-1 and {alpha}-actinin function together to stabilize actin filaments and promote muscle structural integrity.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-06-0584) on March 4, 2009.

Address correspondence to: Mary C. Beckerle (mary.beckerle{at}hci.utah.edu).




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