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Structure paper

TitleThe kinesin-5 tail domain directly modulates the mechanochemical cycle of the motor domain for anti-parallel microtubule sliding.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJan 20, 2020
AuthorsTatyana Bodrug / Elizabeth M Wilson-Kubalek / Stanley Nithianantham / Alex F Thompson / April Alfieri / Ignas Gaska / Jennifer Major / Garrett Debs / Sayaka Inagaki / Pedro Gutierrez / Larisa Gheber / Richard J McKenney / Charles Vaughn Sindelar / Ronald Milligan / Jason Stumpff / Steven S Rosenfeld / Scott T Forth / Jawdat Al-Bassam /
PubMed AbstractKinesin-5 motors organize mitotic spindles by sliding apart microtubules. They are homotetramers with dimeric motor and tail domains at both ends of a bipolar minifilament. Here, we describe a ...Kinesin-5 motors organize mitotic spindles by sliding apart microtubules. They are homotetramers with dimeric motor and tail domains at both ends of a bipolar minifilament. Here, we describe a regulatory mechanism involving direct binding between tail and motor domains and its fundamental role in microtubule sliding. Kinesin-5 tails decrease microtubule-stimulated ATP-hydrolysis by specifically engaging motor domains in the nucleotide-free or ADP states. Cryo-EM reveals that tail binding stabilizes an open motor domain ATP-active site. Full-length motors undergo slow motility and cluster together along microtubules, while tail-deleted motors exhibit rapid motility without clustering. The tail is critical for motors to zipper together two microtubules by generating substantial sliding forces. The tail is essential for mitotic spindle localization, which becomes severely reduced in tail-deleted motors. Our studies suggest a revised microtubule-sliding model, in which kinesin-5 tails stabilize motor domains in the microtubule-bound state by slowing ATP-binding, resulting in high-force production at both homotetramer ends.
External linksElife / PubMed:31958056 / PubMed Central
MethodsEM (helical sym.)
Resolution4.4 Å
Structure data

21314

6vpo

EMDB-21314, PDB-6vpo:
Cryo-EM structure of microtubule-bound KLP61F motor domain in the AMPPNP state
Method: EM (helical sym.) / Resolution: 4.4 Å

21315

6vpp

EMDB-21315, PDB-6vpp:
Cryo-EM structure of microtubule-bound KLP61F motor with tail domain in the nucleotide-free state
Method: EM (helical sym.) / Resolution: 4.4 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • sus scrofa (pig)
  • drosophila melanogaster (fruit fly)
KeywordsMOTOR PROTEIN / Kinesin-5 / microtubules / mitotic spindles / AMPPNP state / cell cycle / KLP61F / nucleotide-free state

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