Zhou, Tiankun, Fleming, Jennifer R, Franke, Barbara, Bogomolovas, Julius, Barsukov, Igor ORCID: 0000-0003-4406-9803, Rigden, Daniel J ORCID: 0000-0002-7565-8937, Labeit, Siegfried and Mayans, Olga
(2016)
CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex.
FEBS LETTERS, 590 (18).
pp. 3098-3110.
Text
FEBSL_CARP_N2A_elements.docx - Author Accepted Manuscript Download (2MB) |
Abstract
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.
Item Type: | Article |
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Uncontrolled Keywords: | circular dichroism, recombinant proteins, SEC-MALLS, small-angle X-ray scattering, X-ray crystallography |
Depositing User: | Symplectic Admin |
Date Deposited: | 30 Aug 2016 10:25 |
Last Modified: | 19 Jan 2023 07:30 |
DOI: | 10.1002/1873-3468.12362 |
Related URLs: | |
URI: | https://livrepository.liverpool.ac.uk/id/eprint/3003069 |