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Aurora B kinase disrupts the extended conformation of lattice-bound Kinesin-13 MCAK

ABSTRACT: We reveal that MCAK has a compact conformation in solution using cross-linking and electron microscopy. When MCAK is bound to the microtubule ends, it adopts an extended conformation with the N terminus and neck region of MCAK interacting with the microtubule. Also Aurora Bphosphorylation does not alter MCAK conformation in solution. Aurora B interferes with the extended conformation of MCAK on microtubules to decrease the affinity of MCAK for microtubules and reduces its depolymerase activity in a graded fashion.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Juan Zou

LAB HEAD: Prof. Juri Rappsilber

PROVIDER: PXD008215 | Pride | 2019-01-07

REPOSITORIES: Pride

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The depolymerase activity of MCAK shows a graded response to Aurora B kinase phosphorylation through allosteric regulation.

McHugh Toni T Zou Juan J Volkov Vladimir A VA Bertin Aurélie A Talapatra Sandeep K SK Rappsilber Juri J Dogterom Marileen M Welburn Julie P I JPI

Journal of cell science 20190114 4

Kinesin-13 motors regulate precise microtubule dynamics and limit microtubule length throughout metazoans by depolymerizing microtubule ends. Recently, the kinesin-13 motor family member MCAK (also known Kif2C) has been proposed to undergo large conformational changes during its catalytic cycle, as it switches from being in solution to being bound to microtubules. Here, we reveal that MCAK has a compact conformation in solution through crosslinking and electron microscopy experiments. When MCAK ...[more]

PMID: 30578316

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