Direct observation of a coil-to-helix contraction triggered by vinculin binding to talin.

ABSTRACT: Vinculin binds unfolded talin domains in focal adhesions, which recruits actin filaments to reinforce the mechanical coupling of this organelle. However, it remains unknown how this interaction is regulated and its impact on the force transmission properties of this mechanotransduction pathway. Here, we use magnetic tweezers to measure the interaction between vinculin head and the talin R3 domain under physiological forces. For the first time, we resolve individual binding events as a short contraction of the unfolded talin polypeptide caused by the reformation of the vinculin-binding site helices, which dictates a biphasic mechanism that regulates this interaction. Force favors vinculin binding by unfolding talin and exposing the vinculin-binding sites; however, the coil-to-helix contract

SUBMITTER: Tapia-Rojo R 

PROVIDER: S-EPMC7244311 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature