CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex



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.

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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
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