Distinct liquid-liquid phase separation properties of end-binding proteins EB1 and EB3.

ABSTRACT: End-binding proteins (EBs) are central components of the network of microtubule-plus-end-tracking proteins (+TIPs) that modulate microtubule dynamics. Recent studies have shown that EBs undergo liquid-liquid phase separation (LLPS), and it was proposed that the resulting condensates could play a major role in the recruitment of other + TIPs as well as in polymerization of tubulin. Here, we performed detailed studies of LLPS properties of two major members of the EB family in mammalian cells, EB1 and EB3. Surprisingly, we found that, despite 67% sequence identity, EB3 has a significantly higher LLPS propensity than EB1, both in vitro and in cells. This difference is due to combined contributions from multiple protein regions, with histidine residues in the N-terminal domain playing a partic

SUBMITTER: Boyko S 

PROVIDER: S-EPMC12661437 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature