Negative regulation of EB1 turnover at microtubule plus ends by interaction with microtubule-associated protein ATIP3.

ABSTRACT: The regulation of microtubule dynamics is critical to ensure essential cell functions. End binding protein 1 (EB1) is a master regulator of microtubule dynamics that autonomously binds an extended GTP/GDP-Pi structure at growing microtubule ends and recruits regulatory proteins at this location. However, negative regulation of EB1 association with growing microtubule ends remains poorly understood. We show here that microtubule-associated tumor suppressor ATIP3 interacts with EB1 through direct binding of a non-canonical proline-rich motif. Results indicate that ATIP3 does not localize at growing microtubule ends and that in situ ATIP3-EB1 molecular complexes are mostly detected in the cytosol. We present evidence that a minimal EB1-interacting sequence of ATIP3 is both necessary and suffi

SUBMITTER: Velot L 

PROVIDER: S-EPMC4791250 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature