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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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2 September 2016
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| In: |
FEBS letters
Year: 2016, Volume: 590, Issue: 18, Pages: 3098-3110 |
| ISSN: | 1873-3468 |
| DOI: | 10.1002/1873-3468.12362 |
| Online Access: | 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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| Author Notes: | Tiankun Zhou, Jennifer R. Fleming, Barbara Franke, Julius Bogomolovas, Igor Barsukov, Daniel J. Rigden, Siegfried Labeit and Olga Mayans |
| Summary: | 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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| Item Description: | Gesehen am 21.09.2019 Available online 2 September 2016 |
| Physical Description: | Online Resource |
| ISSN: | 1873-3468 |
| DOI: | 10.1002/1873-3468.12362 |