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Published online 11 December 2006. doi:10.1083/jcb.200608043
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 175, Number 6, 853-859
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 UNC-98 links an integrin-associated complex to thick filaments in Caenorhabditis elegans muscle

Rachel K. Miller1,2, Hiroshi Qadota1, Megan L. Landsverk3,4, Kristina B. Mercer1, Henry F. Epstein4, and Guy M. Benian1

1 Department of Pathology and 2 Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, GA 30322
3 Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030
4 Department of Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX 77555

Correspondence to Guy M. Benian: pathgb{at}emory.edu

Focal adhesions are multiprotein assemblages that link cells to the extracellular matrix. The transmembrane protein, integrin, is a key component of these structures. In vertebrate muscle, focal adhesion–like structures called costameres attach myofibrils at the periphery of muscle cells to the cell membrane. In Caenorhabditis elegans muscle, all the myofibrils are attached to the cell membrane at both dense bodies (Z-disks) and M-lines. Clustered at the base of dense bodies and M-lines, and associated with the cytoplasmic tail of ß-integrin, is a complex of many proteins, including UNC-97 (vertebrate PINCH). Previously, we showed that UNC-97 interacts with UNC-98, a 37-kD protein, containing four C2H2 Zn fingers, that localizes to M-lines. We report that UNC-98 also interacts with the C-terminal portion of a myosin heavy chain. Multiple lines of evidence support a model in which UNC-98 links integrin-associated proteins to myosin in thick filaments at M-lines.

Abbreviation used in this paper: MHC, myosin heavy chain.


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