Journal
ELIFE
Volume 6, Issue -, Pages -Publisher
eLIFE SCIENCES PUBL LTD
DOI: 10.7554/eLife.27793
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Categories
Funding
- European Commission
- Medical Research Council [MR/J003867/1, MR/M019292/1, MR/J000973/1]
- American Heart Association [SDG20480032]
- National Institute of General Medical Sciences [GM102875, N5073610]
- Centre National de la Re-cherche Scientifique
- Agence Nationale de la Re-cherche [ANR-15-CE13-0017-01]
- Ligue Contre le Cancer [RS14/75-28]
- Instruct-pilote
- Australian Research Council [PJA 20151203285]
- Institut National Du Cancer [2016-1-PL BIO-ICR-1]
- Marie Curie Fellowship [FP7-PEOPLE-2012-IIF]
- BBSRC [BB/K01692X/1] Funding Source: UKRI
- MRC [G0600084, MR/J000973/1, MR/M019292/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K01692X/1] Funding Source: researchfish
- Medical Research Council [MR/J000973/1, 1649825, MR/M019292/1, G0600084] Funding Source: researchfish
- Agence Nationale de la Recherche (ANR) [ANR-15-CE13-0017] Funding Source: Agence Nationale de la Recherche (ANR)
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MKLP2, a kinesin-6, has critical roles during the metaphase-anaphase transition and cytokinesis. Its motor domain contains conserved nucleotide binding motifs, but is divergent in sequence (similar to 35% identity) and size (similar to 40% larger) compared to other kinesins. Using cryo-electron microscopy and biophysical assays, we have undertaken a mechanochemical dissection of the microtubule-bound MKLP2 motor domain during its ATPase cycle, and show that many facets of its mechanism are distinct from other kinesins. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. Furthermore, the footprint of the MKLP2 motor domain on the MT surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences. The conformation of the highly extended loop6 insertion characteristic of kinesin-6s is nucleotide-independent and does not contact the MT surface. Our results emphasize the role of family-specific insertions in modulating kinesin motor function.
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