henhaobio
Sign in

bioRxivBiophysics

Microtubule minus-end aster organization is driven by processive HSET-tubulin clusters

S. R. Norris, S. Jung, P. Singh, C. E. Strothman, A. L. Erwin, M. D. Ohi, M. Zanic, R. Ohi

PDFDOIPreprint

Abstract

Higher-order structures of the microtubule (MT) cytoskeleton are comprised of two architectures: bundles and asters. Although both architectures are critical for cellular function, the molecular pathways that drive aster formation are poorly understood. Here, we study aster formation by human minus-end directed kinesin-14 (HSET/KIFC1). We show that HSET is incapable of forming asters from pre-formed, non-growing MTs, but rapidly forms MT asters in the presence of soluble tubulin. HSET binds soluble (non-polymer) tubulin via its N-terminal tail domain to form heterogeneous HSET-tubulin \"clusters\" containing multiple motors. Cluster formation induces motor processivity and rescues the formation of asters from non-growing MTs. We then show that excess soluble tubulin stimulates aster formation in HeLa cells overexpressing HSET during mitosis. We propose a model where HSET can toggle between MT bundle and aster formation in a manner governed by the availability of soluble tubulin.

Reproducibility ledger

Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.

Sign in to file a reproducibility report.