CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex
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 betwe...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2 September 2016
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| In: |
FEBS letters
Year: 2016, Jahrgang: 590, Heft: 18, Pages: 3098-3110 |
| ISSN: | 1873-3468 |
| DOI: | 10.1002/1873-3468.12362 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1002/1873-3468.12362 Verlag, Volltext: http://febs.onlinelibrary.wiley.com/doi/abs/10.1002/1873-3468.12362 
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| Verfasserangaben: | Tiankun Zhou, Jennifer R. Fleming, Barbara Franke, Julius Bogomolovas, Igor Barsukov, Daniel J. Rigden, Siegfried Labeit and Olga Mayans |
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| 245 | 1 | 0 | |a CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex |c Tiankun Zhou, Jennifer R. Fleming, Barbara Franke, Julius Bogomolovas, Igor Barsukov, Daniel J. Rigden, Siegfried Labeit and Olga Mayans |
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| 520 | |a 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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