An open-pore structure of the mechanosensitive channel MscL derived by determining transmembrane domain interactions upon gating.

ABSTRACT: Mechanosensation, the ability to detect mechanical forces, underlies the senses of hearing, balance, touch, and pain, as well as renal and cardiovascular regulation. Although the sensors are thought to be channels, relatively little is known about eukaryotic mechanosensitive channels or their molecular mechanisms. Thus, because of its tractable nature, a bacterial mechanosensitive channel that serves as an in vivo osmotic "emergency release valve," MscL, has become a paradigm of how a mechanosensitive channel can sense and respond to membrane tension. Here, we have determined the structural rearrangements and interactions between transmembrane domains of MscL that occur upon gating. We utilize an electrostatic repulsion test: If two residues approach upon gating we predicted that substitut

SUBMITTER: Li Y 

PROVIDER: S-EPMC2704598 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature