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The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling
The Z-disc, appearing as a fine dense line forming sarcomere boundaries in striated muscles, when studied in detail reveals crosslinked filament arrays that transmit tension and house myriads of proteins with diverse functions. At the Z-disc the barbed ends of the antiparallel actin filaments from a...
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Formato: | Texto |
Lenguaje: | English |
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Springer Netherlands
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2799012/ https://www.ncbi.nlm.nih.gov/pubmed/19830582 http://dx.doi.org/10.1007/s10974-009-9189-6 |
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author | Luther, Pradeep K. |
author_facet | Luther, Pradeep K. |
author_sort | Luther, Pradeep K. |
collection | PubMed |
description | The Z-disc, appearing as a fine dense line forming sarcomere boundaries in striated muscles, when studied in detail reveals crosslinked filament arrays that transmit tension and house myriads of proteins with diverse functions. At the Z-disc the barbed ends of the antiparallel actin filaments from adjoining sarcomeres interdigitate and are crosslinked primarily by layers of α-actinin. The Z-disc is therefore the site of polarity reversal of the actin filaments, as needed to interact with the bipolar myosin filaments in successive sarcomeres. The layers of α-actinin determine the Z-disc width: fast fibres have narrow (~30–50 nm) Z-discs and slow and cardiac fibres have wide (~100 nm) Z-discs. Comprehensive reviews on the roles of the numerous proteins located at the Z-disc in signalling and disease have been published; the aim here is different, namely to review the advances in structural aspects of the Z-disc. |
format | Text |
id | pubmed-2799012 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-27990122009-12-30 The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling Luther, Pradeep K. J Muscle Res Cell Motil Review Paper The Z-disc, appearing as a fine dense line forming sarcomere boundaries in striated muscles, when studied in detail reveals crosslinked filament arrays that transmit tension and house myriads of proteins with diverse functions. At the Z-disc the barbed ends of the antiparallel actin filaments from adjoining sarcomeres interdigitate and are crosslinked primarily by layers of α-actinin. The Z-disc is therefore the site of polarity reversal of the actin filaments, as needed to interact with the bipolar myosin filaments in successive sarcomeres. The layers of α-actinin determine the Z-disc width: fast fibres have narrow (~30–50 nm) Z-discs and slow and cardiac fibres have wide (~100 nm) Z-discs. Comprehensive reviews on the roles of the numerous proteins located at the Z-disc in signalling and disease have been published; the aim here is different, namely to review the advances in structural aspects of the Z-disc. Springer Netherlands 2009-10-15 2009 /pmc/articles/PMC2799012/ /pubmed/19830582 http://dx.doi.org/10.1007/s10974-009-9189-6 Text en © The Author(s) 2009 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Review Paper Luther, Pradeep K. The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling |
title | The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling |
title_full | The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling |
title_fullStr | The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling |
title_full_unstemmed | The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling |
title_short | The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling |
title_sort | vertebrate muscle z-disc: sarcomere anchor for structure and signalling |
topic | Review Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2799012/ https://www.ncbi.nlm.nih.gov/pubmed/19830582 http://dx.doi.org/10.1007/s10974-009-9189-6 |
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