James M ErvastiSummaryAffiliation: University of Wisconsin Country: USA Publications
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Publications
Costameres: the Achilles' heel of Herculean muscleJames M Ervasti
Department of Physiology, University of Wisconsin Medical School, Madison 53706, USA
J Biol Chem 278:13591-4. 2003- Dystrophin, its interactions with other proteins, and implications for muscular dystrophyJames M Ervasti
Department of Physiology, 127 Service Memorial Institute, University of Wisconsin Medical School, 1300 University Avenue, Madison, WI 53706, USA
Biochim Biophys Acta 1772:108-17. 2007..The dystrophin homologue utrophin can compensate at the cell/tissue level for dystrophin deficiency, but functions through distinct molecular mechanisms of protein-protein interaction... 
Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscleInna N Rybakova
Department of Physiology, University of Wisconsin Medical School, Madison 53706, USA
Mol Biol Cell 13:1512-21. 2002..More generally, our results raise the possibility that spectrin-like repeats may enable some members of the plakin family of cytolinkers to laterally bind and stabilize actin filaments...- Dystrophin and utrophin bind actin through distinct modes of contactInna N Rybakova
Department of Physiology, University of Wisconsin Medical School, 127 Service Memorial Institute, 1300 University Avenue, Madison, WI 53706, USA
J Biol Chem 281:9996-10001. 2006..Finally, we reassessed the abundance of dystrophin in striated muscle using full-length protein as the standard and measured greater than 10-fold higher values than previously reported... - Cytoplasmic gamma-actin contributes to a compensatory remodeling response in dystrophin-deficient muscleLaurin M Hanft
Department of Physiology, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA
Proc Natl Acad Sci U S A 103:5385-90. 2006..However, the presence of excessive myoplasmic gamma-actin may also contribute to altered cell signaling or gene expression in dystrophin-deficient muscle... - Brain alpha-dystroglycan displays unique glycoepitopes and preferential binding to laminin-10/11Erin L McDearmon
Department of Physiology, University of Wisconsin, Madison, 53706, USA
FEBS Lett 580:3381-5. 2006..Our results suggest that tissue-specific glycosylation modifies the laminin binding specificity of alpha-dystroglycan... - Cytoplasmic gamma-actin is not required for skeletal muscle development but its absence leads to a progressive myopathyKevin J Sonnemann
Program in Cellular and Molecular Biology, University of Wisconsin Madison, 53706, USA
Dev Cell 11:387-97. 2006.... - Destabilization of the dystrophin-glycoprotein complex without functional deficits in alpha-dystrobrevin null muscleTina M Bunnell
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota, United States of America
PLoS ONE 3:e2604. 2008..Our results demonstrate that myofiber degeneration alone does not cause functional deficits and suggests that more complex pathological factors contribute to the development of muscle weakness in muscular dystrophy... - Expression of Dp260 in muscle tethers the actin cytoskeleton to the dystrophin-glycoprotein complex and partially prevents dystrophyLaura E Warner
Department of Neurology, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195, USA
Hum Mol Genet 11:1095-105. 2002..We suggest that a non-mechanical defect, attributed to the loss of the N terminus of dystrophin, is likely responsible for the residual dystrophy observed... - Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10Hiroyuki Ido
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan
J Biol Chem 279:10946-54. 2004.... - Core 1 glycans on alpha-dystroglycan mediate laminin-induced acetylcholine receptor clustering but not laminin bindingErin L McDearmon
Graduate Program in Molecular and Cellular Pharmacology, University of Wisconsin-Madison Medical School, 53706, USA
J Biol Chem 278:44868-73. 2003.... - The utrophin actin-binding domain binds F-actin in two different modes: implications for the spectrin superfamily of proteinsVitold E Galkin
Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA
J Cell Biol 157:243-51. 2002..The cell may use the modular CH domains found in the spectrin superfamily of actin-binding proteins to bind actin in manifold ways, allowing for complexity to arise from the interactions of a relatively few simple modules with actin... - Cytoplasmic gamma-actin expression in diverse animal models of muscular dystrophyLaurin M Hanft
Department of Physiology, University of Wisconsin, Madison, WI, United States
Neuromuscul Disord 17:569-74. 2007..These data suggest that elevated gamma(cyto)-actin is part of a compensatory cytoskeletal remodeling program that may partially stabilize dystrophic muscle in some cases where the dystrophin-glycoprotein complex is compromised... 
Biology of the striated muscle dystrophin-glycoprotein complexJames M Ervasti
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Int Rev Cytol 265:191-225. 2008..Studies in model organisms confirm the importance of the dystrophin-glycoprotein complex for muscle cell viability and have provided new leads toward a full understanding of its secondary roles in muscle biology...- Skeletal muscle-specific ablation of gamma(cyto)-actin does not exacerbate the mdx phenotypeKurt W Prins
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota, United States of America
PLoS ONE 3:e2419. 2008.... - Contributions of the LG modules and furin processing to laminin-2 functionsSergei P Smirnov
Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA
J Biol Chem 277:18928-37. 2002....