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Titin-dependent biomechanical feedback tailors sarcomeres to specialised muscle functions in insects

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Loreau, Vincent | Koolhaas, Wouter | Chan, Eunice, Hoyee | de Boissier, Paul | Brouilly, Nicolas | Avosani, Sabina | Sane, Aditya | Pitaval, Christophe | Reiter, Stefanie | Luis, Nuno, Miguel | Mangeol, Pierre | von Philipsborn, Anne, C | Rupprecht, Jean-François | Görlich, Dirk | Habermann, Bianca, H | Schnorrer, Frank

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Sarcomeres are the contractile units of muscles that enable animals to move. Insect muscles are remarkable examples because they use extremely different contraction frequencies (ranging from ∼1 to 1000 Hz) and amplitudes for flying, walking and crawling. This is puzzling because sarcomeres are built from essentially the same actin-myosin components. We show here that the giant protein titin is the key to this functional specialisation. I-band titin spans and determines the length of the sarcomeric I-band, and occurs in muscle-type-specific isoforms. Surprisingly, it also rules the length of the force-generating myosin filament in a force feedback mechanism, even though it is not present there. We provide evidence for this model and its validity beyond insects.

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