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Fishing out proteins that bind to titin
Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but prese...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2001
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196855/ https://www.ncbi.nlm.nih.gov/pubmed/11448986 http://dx.doi.org/10.1083/jcb.200106072 |
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author | Sanger, Joseph W. Sanger, Jean M. |
author_facet | Sanger, Joseph W. Sanger, Jean M. |
author_sort | Sanger, Joseph W. |
collection | PubMed |
description | Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but present at about one tenth the level (Young et al., 2001). Like titin, obscurin contains multiple immunoglobulin-like domains linked in tandem, but in contrast to titin it contains just two fibronectin-like domains. It also contains sequences that suggest obscurin may have roles in signal transduction. During embryonic development, its localization changes from the Z-band to the M-band. With these intriguing properties, obscurin may not remain obscure for long. |
format | Text |
id | pubmed-2196855 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2001 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21968552008-05-01 Fishing out proteins that bind to titin Sanger, Joseph W. Sanger, Jean M. J Cell Biol Reviews Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but present at about one tenth the level (Young et al., 2001). Like titin, obscurin contains multiple immunoglobulin-like domains linked in tandem, but in contrast to titin it contains just two fibronectin-like domains. It also contains sequences that suggest obscurin may have roles in signal transduction. During embryonic development, its localization changes from the Z-band to the M-band. With these intriguing properties, obscurin may not remain obscure for long. The Rockefeller University Press 2001-07-09 /pmc/articles/PMC2196855/ /pubmed/11448986 http://dx.doi.org/10.1083/jcb.200106072 Text en Copyright © 2001, The Rockefeller University Press 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 | Reviews Sanger, Joseph W. Sanger, Jean M. Fishing out proteins that bind to titin |
title | Fishing out proteins that bind to titin |
title_full | Fishing out proteins that bind to titin |
title_fullStr | Fishing out proteins that bind to titin |
title_full_unstemmed | Fishing out proteins that bind to titin |
title_short | Fishing out proteins that bind to titin |
title_sort | fishing out proteins that bind to titin |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196855/ https://www.ncbi.nlm.nih.gov/pubmed/11448986 http://dx.doi.org/10.1083/jcb.200106072 |
work_keys_str_mv | AT sangerjosephw fishingoutproteinsthatbindtotitin AT sangerjeanm fishingoutproteinsthatbindtotitin |