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Author Notes:

Correspondence to Guy M. Benian: pathgb@emory.edu

We thank Pam Hoppe and Bob Waterston for worm strain RW1596 and Bob Barstead for RB2, a random primed C. elegans cDNA library. We thank Dan Kalman and Krishna Bhat for the use of their deconvolution and confocal microscope systems. We also thank Denise Flaherty and Maureen Powers for advice on methods of protein purification, ELISA, and microscopy. Some strains used in this work were provided by the Caenorhabditis Genetics Center, which is supported by the National Center for Research Resources of the National Institutes of Health.

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Research Funding:

This work was supported by grants from the National Institutes of Health to G.M. Benian (AR051466 and AR052133), a predoctoral fellowship from the American Heart Association Southeast Affiliate to R.K. Miller (0415274B), and by grants from the National Institutes of Health (AR0500051) and the Muscular Dystrophy Association to H.F. Epstein.

Keywords:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Cell Biology
  • MYOSIN HEAVY-CHAIN
  • BODY-WALL MUSCLE
  • ADHESION COMPLEXES
  • PROTEIN
  • PARAMYOSIN
  • FILAMENTS
  • GENE
  • IDENTIFICATION
  • LOCALIZATION
  • COSTAMERES

UNC-98 links an integrin-associated complex to thick laments in Caenorhabditis elegans muscle

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Journal Title:

Journal of Cell Biology

Volume:

Volume 175, Number 6

Publisher:

, Pages 853-859

Type of Work:

Article | Final Publisher PDF

Abstract:

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 β-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. © The Rockefeller University Press.

Copyright information:

© 2006, The Rockefeller University Press.

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