Geometry of antiparallel microtubule bundles regulates relative sliding and stalling by PRC1 and Kif4A.

ABSTRACT: Motor and non-motor crosslinking proteins play critical roles in determining the size and stability of microtubule-based architectures. Currently, we have a limited understanding of how geometrical properties of microtubule arrays, in turn, regulate the output of crosslinking proteins. Here we investigate this problem in the context of microtubule sliding by two interacting proteins: the non-motor crosslinker PRC1 and the kinesin Kif4A. The collective activity of PRC1 and Kif4A also results in their accumulation at microtubule plus-ends ('end-tag'). Sliding stalls when the end-tags on antiparallel microtubules collide, forming a stable overlap. Interestingly, we find that structural properties of the initial array regulate microtubule organization by PRC1-Kif4A. First, sliding velocity sca

SUBMITTER: Wijeratne S 

PROVIDER: S-EPMC6200392 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature