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

DOI: 10.1002/1873-3468.12362 DOI Help

Authors: Tiankun Zhou (University of Konstanz; University of Liverpool) , Jennifer R. Fleming (University of Konstanz; University of Liverpool) , Barbara Franke (University of Konstanz) , Julijus Bogomolovas (University of Heidelberg) , Igor Barsukov (Institute of Integrative Biology, University of Liverpool) , Daniel J. Rigden (Institute of Integrative Biology, University of Liverpool) , Siegfried Labeit (University of Heidelberg) , Olga Mayans (University of Konstanz; University of Liverpool)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters

State: Published (Approved)
Published: September 2016
Diamond Proposal Number(s): 12788

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.

Journal Keywords: circular dichroism; recombinant proteins; SEC-MALLS; small-angle X-ray scattering; X-ray crystallography

Diamond Keywords: Cardiovascular Disease

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: B21-High Throughput SAXS

Added On: 20/09/2016 15:17

Discipline Tags:

Non-Communicable Diseases Health & Wellbeing Biochemistry Chemistry Biophysics Life Sciences & Biotech

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)