Evidence map›Paper›PMID 41648279›Full record

ArticlebioRxiv : the preprint server for biology2026

A Phosphorylation Switch Governs KIF11's Mechanical Output During Mitosis.

Amila Šemić, Babu J N Reddy, Joseph M Muretta, Sarah E Vandal, Alex F Thompson, Cindy L Fonseca, Steven S Rosenfeld, Steven P Gross, Jason Stumpff

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Amila ŠemićDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Babu J N ReddyDepartment of Developmental and Cell Biology, University of California, Irvine, CA 92697.
Joseph M MurettaDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455.
Sarah E VandalDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Alex F ThompsonDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Cindy L FonsecaDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Steven S RosenfeldDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Jacksonville, FL 32224.
Steven P GrossDepartment of Developmental and Cell Biology, University of California, Irvine, CA 92697.
Jason StumpffDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.ORCID 0000-0003-0392-1254

Funding

Mechanisms of microtubule motors and chromosome segregationR35GM144133 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI JASON K STUMPFF · 2022 to 2026
$2.4M
Tuning Mitotic Kinesins Through Motor Domain Post Translational ModificationsR01GM130556 · NIGMS · MAYO CLINIC JACKSONVILLE · PI GROSS, STEVEN P, MURETTA, JOSEPH M. · 2019 to 2022
$2.4M
Molecular Etiology of Spondyloepimetaphyseal Dysplasia with Joint Laxity - Leptodactylic TypeF31AR074887 · NIAMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI THOMPSON, ALEX · 2019 to 2021
$100k
NIAMS NIH HHS F31 AR074887NIGMS NIH HHS R01 GM130556NIGMS NIH HHS R35 GM144133
6 · The paper itself

Abstract

The kinesin-5 motor protein KIF11 is crucial for mitotic spindle assembly, driving the separation of spindle poles through microtubule sliding. Src-family kinases phosphorylate KIF11 at multiple tyrosine residues within its motor domain, but the mechanistic consequences of these modifications remain unclear. Here, we dissect the role of phosphorylation at Y211 using phospho-mimetic (Y211E) and non-phosphorylatable mutants (Y211F) in biochemical, biophysical, and cellular assays. Optical trapping and Förster resonance energy transfer (FRET) analyses reveal that Y211 phosphorylation slows neck-linker docking, reducing motor velocity and force generation under load. In human cells, Y211E expression impairs bipolar spindle formation and decreases spindle pole separation velocity, while Y211F shortens steady-state spindle length. Fluorescence recovery after photobleaching (FRAP) analyses show that Y211E accelerates motor turnover on spindle microtubules, consistent with the mutant motor's heightened load sensitivity. Together, these findings support a model in which Src-mediated phosphorylation at Y211 acts as a rheostat to tune KIF11 mechanochemistry and spindle assembly dynamics, linking cancer-relevant kinase signaling to mitotic force generation.

Identifiers

PMID41648279
PMCPMC12871612

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.