Interaction between the mitochondrial adaptor MIRO and the motor adaptor TRAK.

ABSTRACT: MIRO (mitochondrial Rho GTPase) consists of two GTPase domains flanking two Ca²⁺-binding EF-hand domains. A C-terminal transmembrane helix anchors MIRO to the outer mitochondrial membrane, where it functions as a general adaptor for the recruitment of cytoskeletal proteins that control mitochondrial dynamics. One protein recruited by MIRO is TRAK (trafficking kinesin-binding protein), which in turn recruits the microtubule-based motors kinesin-1 and dynein-dynactin. The mechanism by which MIRO interacts with TRAK is not well understood. Here, we map and quantitatively characterize the interaction of human MIRO1 and TRAK1 and test its potential regulation by Ca²⁺ and/or GTP binding. TRAK1 binds MIRO1 with low micromolar affinity. The interaction was mapped to a fragmen

SUBMITTER: Baltrusaitis EE 

PROVIDER: S-EPMC10746525 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature