Small Heat Shock proteins such as HspB1 are molecular chaperones in charge of preventing harmful misfolding of proteins under stress conditions. Work led by the Benesch and Gehmlich groups shows, from muscle fibers down to single molecules, that phosphorylation of HspB1 alters its intramolecular dynamics, facilitating its binding to the mechanosensitive Filamin C. In good correspondence with NMR data, our calculations reveal that over over the course of microsecond-long simulations the N-terminus of HspB1 detaches from the rest of the protein.

Collier M.T., Alderson, T.R., de Villiers, C.P., Nicholls, D. , Gastall, H.Y., Allison, T.M., Degiacomi M.T., Jiang, H., Mlynek, G., Fürst, D.O., van der Ven, P.F.M., Djinovic-Carugo, K., Baldwin, A.J., Watkins, H., Gehmlich, K., Benesch, J.L.P. (2019), HspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C. Science Advances, 5(5)