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A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors

Muscle cells infected at the permissive temperature with temperature- sensitive mutants of Rous sarcoma virus and shifted to the non- permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci....

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1988
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115064/
https://www.ncbi.nlm.nih.gov/pubmed/2836437
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description Muscle cells infected at the permissive temperature with temperature- sensitive mutants of Rous sarcoma virus and shifted to the non- permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci. USA. 81:2265-2269). Work described in this paper demonstrates that the virally-infected cells are missing a 37-kD peptide which reacts with an anti-tropomyosin antiserum. Using a monoclonal antibody specific for the missing peptide, we show that this tropomyosin is absent from fibroblasts and is distinct from smooth muscle tropomyosins. It is also different from the two previously identified striated muscle myofibrillar tropomyosins (alpha and beta). We suggest that, in normal muscle, this novel, non-myofibrillar, tropomyosin-like molecule is an important component of a cytoskeletal network necessary for cluster formation.
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spelling pubmed-21150642008-05-01 A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors J Cell Biol Articles Muscle cells infected at the permissive temperature with temperature- sensitive mutants of Rous sarcoma virus and shifted to the non- permissive temperature form myotubes that are unable to cluster acetylcholine receptors (Anthony, D. T., S. M. Schuetze, and L. L. Rubin. 1984. Proc. Natl. Acad. Sci. USA. 81:2265-2269). Work described in this paper demonstrates that the virally-infected cells are missing a 37-kD peptide which reacts with an anti-tropomyosin antiserum. Using a monoclonal antibody specific for the missing peptide, we show that this tropomyosin is absent from fibroblasts and is distinct from smooth muscle tropomyosins. It is also different from the two previously identified striated muscle myofibrillar tropomyosins (alpha and beta). We suggest that, in normal muscle, this novel, non-myofibrillar, tropomyosin-like molecule is an important component of a cytoskeletal network necessary for cluster formation. The Rockefeller University Press 1988-05-01 /pmc/articles/PMC2115064/ /pubmed/2836437 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors
title A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors
title_full A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors
title_fullStr A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors
title_full_unstemmed A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors
title_short A molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors
title_sort molecular defect in virally transformed muscle cells that cannot cluster acetylcholine receptors
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115064/
https://www.ncbi.nlm.nih.gov/pubmed/2836437