Publikation: CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex
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2016
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Bogomolovas, Julius
Barsukov, Igor
Rigden, Daniel J.
Labeit, Siegfried
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FEBS Letters. 2016, 590(18), pp. 3098-3110. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1002/1873-3468.12362
Zusammenfassung
The cardiac ankyrin repeat protein (CARP) is up-regulated in the myocardium during cardiovascular disease and in response to mechanical or toxic stress. Stress-induced CARP interacts with the N2A spring region of the titin filament to modulate muscle compliance. We characterize the interaction between CARP and titin-N2A and show that the binding site in titin spans the dual domain UN2A-Ig81. We find that the unique sequence UN2A is not structurally disordered, but that it has a stable, elongated α-helical fold that possibly acts as a constant force spring. Our findings portray CARP/titin-N2A as a structured node and help to rationalize the molecular basis of CARP mechanosensing in the sarcomeric I-band.
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570 Biowissenschaften, Biologie
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ZHOU, Tiankun, Jennifer R. FLEMING, Barbara FRANKE, Julius BOGOMOLOVAS, Igor BARSUKOV, Daniel J. RIGDEN, Siegfried LABEIT, Olga MAYANS, 2016. CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex. In: FEBS Letters. 2016, 590(18), pp. 3098-3110. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1002/1873-3468.12362BibTex
@article{Zhou2016-09inter-36547,
year={2016},
doi={10.1002/1873-3468.12362},
title={CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex},
number={18},
volume={590},
issn={0014-5793},
journal={FEBS Letters},
pages={3098--3110},
author={Zhou, Tiankun and Fleming, Jennifer R. and Franke, Barbara and Bogomolovas, Julius and Barsukov, Igor and Rigden, Daniel J. and Labeit, Siegfried and Mayans, Olga}
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<dcterms:abstract xml:lang="eng">The cardiac ankyrin repeat protein (CARP) is up-regulated in the myocardium during cardiovascular disease and in response to mechanical or toxic stress. Stress-induced CARP interacts with the N2A spring region of the titin filament to modulate muscle compliance. We characterize the interaction between CARP and titin-N2A and show that the binding site in titin spans the dual domain UN2A-Ig81. We find that the unique sequence UN2A is not structurally disordered, but that it has a stable, elongated α-helical fold that possibly acts as a constant force spring. Our findings portray CARP/titin-N2A as a structured node and help to rationalize the molecular basis of CARP mechanosensing in the sarcomeric I-band.</dcterms:abstract>
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