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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS	CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex Tiankun Zhou , Jennifer R. Fleming , Barbara Franke , Julijus Bogomolovas , Igor Barsukov , Daniel J. Rigden , Siegfried Labeit , Olga Mayans Febs Letters DOI: 10.1002/1873-3468.12362 Diamond Proposal Number(s): [12788] Show Abstract ▼ 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.	Sep 2016

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