Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes
Protein phosphatase 5 (PP5) is expressed in many cell types but its role in cardiomyocytes is unknown. Here the authors show that PP5 binds and dephosphorylates elastic titin in cardiac sarcomeres, and that PP5 is increased in heart failure, reducing cardiomyocyte compliance.
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2018-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-02483-3 |
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doaj-cf31000b822e4204a0bb95e237b05a562021-05-11T09:35:19ZengNature Publishing GroupNature Communications2041-17232018-01-019111410.1038/s41467-017-02483-3Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytesJudith Krysiak0Andreas Unger1Lisa Beckendorf2Nazha Hamdani3Marion von Frieling-Salewsky4Margaret M. Redfield5Cris G. dos Remedios6Farah Sheikh7Ulrich Gergs8Peter Boknik9Wolfgang A. Linke10Department of Cardiovascular Physiology, Ruhr University BochumDepartment of Cardiovascular Physiology, Ruhr University BochumDepartment of Cardiovascular Physiology, Ruhr University BochumDepartment of Cardiovascular Physiology, Ruhr University BochumInstitute of Physiology II, University of MuensterDivision of Cardiovascular Diseases, Mayo ClinicDepartment of Anatomy & Histology, University of SydneyDepartment of Medicine, University of California-San DiegoInstitute for Pharmacology and Toxicology, University of Halle-WittenbergInstitute for Pharmacology and Toxicology, University of MuensterInstitute of Physiology II, University of MuensterProtein phosphatase 5 (PP5) is expressed in many cell types but its role in cardiomyocytes is unknown. Here the authors show that PP5 binds and dephosphorylates elastic titin in cardiac sarcomeres, and that PP5 is increased in heart failure, reducing cardiomyocyte compliance.https://doi.org/10.1038/s41467-017-02483-3 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Judith Krysiak Andreas Unger Lisa Beckendorf Nazha Hamdani Marion von Frieling-Salewsky Margaret M. Redfield Cris G. dos Remedios Farah Sheikh Ulrich Gergs Peter Boknik Wolfgang A. Linke |
spellingShingle |
Judith Krysiak Andreas Unger Lisa Beckendorf Nazha Hamdani Marion von Frieling-Salewsky Margaret M. Redfield Cris G. dos Remedios Farah Sheikh Ulrich Gergs Peter Boknik Wolfgang A. Linke Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes Nature Communications |
author_facet |
Judith Krysiak Andreas Unger Lisa Beckendorf Nazha Hamdani Marion von Frieling-Salewsky Margaret M. Redfield Cris G. dos Remedios Farah Sheikh Ulrich Gergs Peter Boknik Wolfgang A. Linke |
author_sort |
Judith Krysiak |
title |
Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes |
title_short |
Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes |
title_full |
Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes |
title_fullStr |
Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes |
title_full_unstemmed |
Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes |
title_sort |
protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2018-01-01 |
description |
Protein phosphatase 5 (PP5) is expressed in many cell types but its role in cardiomyocytes is unknown. Here the authors show that PP5 binds and dephosphorylates elastic titin in cardiac sarcomeres, and that PP5 is increased in heart failure, reducing cardiomyocyte compliance. |
url |
https://doi.org/10.1038/s41467-017-02483-3 |
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