Evidence map›Paper›PMID 34940839›Full record

ArticleDevelopment (Cambridge, England)2021

A stop or go switch: glycogen synthase kinase 3β phosphorylation of the kinesin 1 motor domain at Ser314 halts motility without detaching from microtubules.

Rupkatha Banerjee, Piyali Chakraborty, Michael C Yu, Shermali Gunawardena

Open access · bronzeAbstract read
In one paragraph

Article in Development (Cambridge, England), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  6. Review
  7. The HSV-1 pUL37 protein promotes cell invasion by regulating the kinesin-1 motor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Disruption of axonal transport in neurodegeneration.The Journal of clinical investigation · 2023
    Review
  12. Review
  13. Review
  14. Review
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Rupkatha BanerjeeDepartment of Biological Sciences, The State University of New York at Buffalo, Buffalo, NY 14260, USA.
Piyali ChakrabortyNeuroscience Graduate Program, The State University of New York at Buffalo, Buffalo, NY 14260, USA.
Michael C YuDepartment of Biological Sciences, The State University of New York at Buffalo, Buffalo, NY 14260, USA.ORCID 0000-0002-3611-9295
Shermali GunawardenaDepartment of Biological Sciences, The State University of New York at Buffalo, Buffalo, NY 14260, USA.ORCID 0000-0001-8776-9397
University at Buffalo, State University of New York · US

Funding

Dissecting the in vivo role of glycogen synthase kinase-3 beta (GSK3b) in the function of kinesin-1 using CRISPR/cas-1R03NS114731 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI GUNAWARDENA, SHERMALI · 2020 to 2020
$157k
NINDS NIH HHS R03 NS114731
6 · The paper itself

Abstract

It is more than 25 years since the discovery that kinesin 1 is phosphorylated by several protein kinases. However, fundamental questions still remain as to how specific protein kinase(s) contribute to particular motor functions under physiological conditions. Because, within an whole organism, kinase cascades display considerable crosstalk and play multiple roles in cell homeostasis, deciphering which kinase(s) is/are involved in a particular process has been challenging. Previously, we found that GSK3β plays a role in motor function. Here, we report that a particular site on kinesin 1 motor domain (KHC), S314, is phosphorylated by GSK3β in vivo. The GSK3β-phosphomimetic-KHCS314D stalled kinesin 1 motility without dissociating from microtubules, indicating that constitutive GSK3β phosphorylation of the motor domain acts as a STOP. In contrast, uncoordinated mitochondrial motility was observed in CRISPR/Cas9-GSK3β non-phosphorylatable-KHCS314A Drosophila larval axons, owing to decreased kinesin 1 attachment to microtubules and/or membranes, and reduced ATPase activity. Together, we propose that GSK3β phosphorylation fine-tunes kinesin 1 movement in vivo via differential phosphorylation, unraveling the complex in vivo regulatory mechanisms that exist during axonal motility of cargos attached to multiple kinesin 1 and dynein motors.

Indexed as

Adenosine TriphosphatasesAnimalsAxonal TransportAxonsCell MovementCRISPR-Cas SystemsDrosophila melanogasterDrosophila ProteinsDyneinsGlycogen Synthase Kinase 3 betaKinesinsLarvaMicrotubulesNeuronsPhosphorylationProtein DomainsAdenosine TriphosphatasesDrosophila ProteinsDyneinsGlycogen Synthase Kinase 3 betaKhc protein, DrosophilaKinesinsAxonal transportCRISPR/Cas9DrosophilaGSK3βKinesin 1PhosphorylationProcessivity

Identifiers

PMID34940839
PMCPMC8722386
OpenAlexW4200198204

What OpenQuestion holds

Textmetadata
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.