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A correction to this article has been published: J. Cell Biol. 153 (4) 889-890
Published online 19 March 2001. doi:10.1083/jcb.152.6.1313
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© The Rockefeller University Press, 0021-9525/2001//1313 $5.00
The Journal of Cell Biology, Volume 152, Number 6, , 2001 1313-1320

Report

The Caenorhabditis elegans unc-78 Gene Encodes a Homologue of Actin-Interacting Protein 1 Required for Organized Assembly of Muscle Actin Filaments



Shoichiro Onoa

a Department of Pathology, Emory University, Atlanta, Georgia 30322
Department of Pathology, Emory University, 1639 Pierce Dr., Woodruff Memorial Building, Room 7109C, Atlanta, GA 30322.(404) 727-8540(404) 727-3916

sono{at}emory.edu

Assembly and maintenance of myofibrils require dynamic regulation of the actin cytoskeleton. In Caenorhabditis elegans, UNC-60B, a muscle-specific actin depolymerizing factor (ADF)/cofilin isoform, is required for proper actin filament assembly in body wall muscle (Ono, S., D.L. Baillie, and G.M. Benian. 1999. J. Cell Biol. 145:491–502). Here, I show that UNC-78 is a homologue of actin-interacting protein 1 (AIP1) and functions as a novel regulator of actin organization in myofibrils. In unc-78 mutants, the striated organization of actin filaments is disrupted, and large actin aggregates are formed in the body wall muscle cells, resulting in defects in their motility. Point mutations in unc-78 alleles change conserved residues within different WD repeats of the UNC-78 protein and cause less severe phenotypes than a deletion allele, suggesting that these mutations partially impair the function of UNC-78. UNC-60B is normally localized in the diffuse cytoplasm and to the myofibrils in wild type but mislocalized to the actin aggregates in unc-78 mutants. Similar Unc-78 phenotypes are observed in both embryonic and adult muscles. Thus, AIP1 is an important regulator of actin filament organization and localization of ADF/cofilin during development of myofibrils.

Key Words: myofibrils • AIP1 • ADF/cofilin • WD repeats • actin filament dynamics

© 2001 The Rockefeller University Press

Abbreviations used in this paper: ADF, actin depolymerizing factor; AIP1, actin-interacting protein 1; PBS-TG, PBS containing 0.5% Triton X-100 and 30 mM glycine.


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