Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.

ABSTRACT: Ankyrins together with their spectrin partners are the master organizers of micron-scale membrane domains in diverse tissues. The 24 ankyrin (ANK) repeats of ankyrins bind to numerous membrane proteins, linking them to spectrin-based cytoskeletons at specific membrane microdomains. The accessibility of the target binding groove of ANK repeats must be regulated to achieve spatially defined functions of ankyrins/target complexes in different tissues, though little is known in this regard. Here we systemically investigated the autoinhibition mechanism of ankyrin-B/G by combined biochemical, biophysical and structural biology approaches. We discovered that the entire ANK repeats are inhibited by combinatorial and quasi-independent bindings of multiple disordered segments located in the ankyrin

SUBMITTER: Chen K 

PROVIDER: S-EPMC5779224 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature