Structural basis of protein condensation on microtubules underlying branching microtubule nucleation.

ABSTRACT: Targeting protein for Xklp2 (TPX2) is a key factor that stimulates branching microtubule nucleation during cell division. Upon binding to microtubules (MTs), TPX2 forms condensates via liquid-liquid phase separation, which facilitates recruitment of microtubule nucleation factors and tubulin. We report the structure of the TPX2 C-terminal minimal active domain (TPX2^α5-α7) on the microtubule lattice determined by magic-angle-spinning NMR. We demonstrate that TPX2^α5-α7 forms a co-condensate with soluble tubulin on microtubules and binds to MTs between two adjacent protofilaments and at the intersection of four tubulin heterodimers. These interactions stabilize the microtubules and promote the recruitment of tubulin. Our results reveal that TPX2^α5-α7 is disord

SUBMITTER: Guo C 

PROVIDER: S-EPMC10284871 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature