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Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations
Nuclear envelopes from liver and a neuroblastoma cell line have previously been analyzed by proteomics; however, most diseases associated with the nuclear envelope affect muscle. To determine whether muscle has unique nuclear envelope proteins, rat skeletal muscle nuclear envelopes were prepared and...
Autores principales: | , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The American Society for Biochemistry and Molecular Biology
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3016689/ https://www.ncbi.nlm.nih.gov/pubmed/20876400 http://dx.doi.org/10.1074/mcp.M110.003129 |
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author | Wilkie, Gavin S. Korfali, Nadia Swanson, Selene K. Malik, Poonam Srsen, Vlastimil Batrakou, Dzmitry G. de las Heras, Jose Zuleger, Nikolaj Kerr, Alastair R. W. Florens, Laurence Schirmer, Eric C. |
author_facet | Wilkie, Gavin S. Korfali, Nadia Swanson, Selene K. Malik, Poonam Srsen, Vlastimil Batrakou, Dzmitry G. de las Heras, Jose Zuleger, Nikolaj Kerr, Alastair R. W. Florens, Laurence Schirmer, Eric C. |
author_sort | Wilkie, Gavin S. |
collection | PubMed |
description | Nuclear envelopes from liver and a neuroblastoma cell line have previously been analyzed by proteomics; however, most diseases associated with the nuclear envelope affect muscle. To determine whether muscle has unique nuclear envelope proteins, rat skeletal muscle nuclear envelopes were prepared and analyzed by multidimensional protein identification technology. Many novel muscle-specific proteins were identified that did not appear in previous nuclear envelope data sets. Nuclear envelope residence was confirmed for 11 of these by expression of fusion proteins and by antibody staining of muscle tissue cryosections. Moreover, transcript levels for several of the newly identified nuclear envelope transmembrane proteins increased during muscle differentiation using mouse and human in vitro model systems. Some of these proteins tracked with microtubules at the nuclear surface in interphase cells and accumulated at the base of the microtubule spindle in mitotic cells, suggesting they may associate with complexes that connect the nucleus to the cytoskeleton. The finding of tissue-specific proteins in the skeletal muscle nuclear envelope proteome argues the importance of analyzing nuclear envelopes from all tissues linked to disease and suggests that general investigation of tissue differences in organellar proteomes might yield critical insights. |
format | Text |
id | pubmed-3016689 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-30166892011-01-18 Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations Wilkie, Gavin S. Korfali, Nadia Swanson, Selene K. Malik, Poonam Srsen, Vlastimil Batrakou, Dzmitry G. de las Heras, Jose Zuleger, Nikolaj Kerr, Alastair R. W. Florens, Laurence Schirmer, Eric C. Mol Cell Proteomics Research Nuclear envelopes from liver and a neuroblastoma cell line have previously been analyzed by proteomics; however, most diseases associated with the nuclear envelope affect muscle. To determine whether muscle has unique nuclear envelope proteins, rat skeletal muscle nuclear envelopes were prepared and analyzed by multidimensional protein identification technology. Many novel muscle-specific proteins were identified that did not appear in previous nuclear envelope data sets. Nuclear envelope residence was confirmed for 11 of these by expression of fusion proteins and by antibody staining of muscle tissue cryosections. Moreover, transcript levels for several of the newly identified nuclear envelope transmembrane proteins increased during muscle differentiation using mouse and human in vitro model systems. Some of these proteins tracked with microtubules at the nuclear surface in interphase cells and accumulated at the base of the microtubule spindle in mitotic cells, suggesting they may associate with complexes that connect the nucleus to the cytoskeleton. The finding of tissue-specific proteins in the skeletal muscle nuclear envelope proteome argues the importance of analyzing nuclear envelopes from all tissues linked to disease and suggests that general investigation of tissue differences in organellar proteomes might yield critical insights. The American Society for Biochemistry and Molecular Biology 2011-01 2010-09-27 /pmc/articles/PMC3016689/ /pubmed/20876400 http://dx.doi.org/10.1074/mcp.M110.003129 Text en © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | Research Wilkie, Gavin S. Korfali, Nadia Swanson, Selene K. Malik, Poonam Srsen, Vlastimil Batrakou, Dzmitry G. de las Heras, Jose Zuleger, Nikolaj Kerr, Alastair R. W. Florens, Laurence Schirmer, Eric C. Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations |
title | Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations |
title_full | Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations |
title_fullStr | Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations |
title_full_unstemmed | Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations |
title_short | Several Novel Nuclear Envelope Transmembrane Proteins Identified in Skeletal Muscle Have Cytoskeletal Associations |
title_sort | several novel nuclear envelope transmembrane proteins identified in skeletal muscle have cytoskeletal associations |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3016689/ https://www.ncbi.nlm.nih.gov/pubmed/20876400 http://dx.doi.org/10.1074/mcp.M110.003129 |
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