Evidence map›Paper›PMID 21385839›Full record

ArticleJournal of cell science2011

Phosphorylation of kinesin light chain 1 at serine 460 modulates binding and trafficking of calsyntenin-1.

Alessio Vagnoni, Lilia Rodriguez, Catherine Manser, Kurt J De Vos, Christopher C J Miller

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

45 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
  5. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Article
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  15. Loss of PDK1 Induces Meiotic Defects in Oocytes From Diabetic Mice.Frontiers in cell and developmental biology · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. Article
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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

5 authors at 1 institution in 1 country.

Alessio VagnoniMRC Centre for Neurodegeneration Research, Institute of Psychiatry, King's College London, PO Box 37, De Crespigny Park, Denmark Hill, London SE5 8AF, UK.
Lilia Rodriguez
Catherine Manser
Kurt J De Vos
Christopher C J Miller
King's College London · GB

Funding

Medical Research Council G0501573Wellcome Trust
6 · The paper itself

Abstract

Kinesin light chain 1 (KLC1) binds to the intracellular cytoplasmic domain of the type-1 membrane-spanning protein calsyntenin-1 (also known as alcadein-α) to mediate transport of a subset of vesicles. Here, we identify serine 460 in KLC1 (KLC1ser460) as a phosphorylation site and show that mutation of KLC1ser460 influences the binding of KLC1 to calsyntenin-1. Mutation of KLC1ser460 to an alanine residue, to preclude phosphorylation, increased the binding of calsyntenin-1, whereas mutation to an aspartate residue, to mimic permanent phosphorylation, reduced the binding. Mutation of KLC1ser460 did not affect the interaction of KLC1 with four other known binding partners: huntingtin-associated protein 1 isoform A (HAP1A), collapsin response mediator protein-2 (CRMP2), c-Jun N-terminal kinase-interacting protein-1 (JIP1) and kinase-D-interacting substrate of 220 kDa (Kidins220). KLC1ser460 is a predicted mitogen-activated protein kinase (MAPK) target site, and we show that extracellular-signal-regulated kinase (ERK) phosphorylates this residue in vitro. We also demonstrate that inhibition of ERK promotes binding of calsyntenin-1 to KLC1. Finally, we show that expression of the KLC1ser460 mutant proteins influences calsyntenin-1 distribution and transport in cultured cells. Thus, phosphorylation of KLC1ser460 represents a mechanism for selectively regulating the binding and trafficking of calsyntenin-1.

Indexed as

Amino Acid MotifsAmino Acid SubstitutionAnimalsCalcium-Binding ProteinsCell LineCHO CellsCricetinaeCricetulusHumansKinesinsMicrotubule-Associated ProteinsPhosphorylationProtein BindingProtein TransportCalcium-Binding ProteinsCLSTN1 protein, humanClstn1 protein, mouseKinesinsKLC1 protein, humanKns2 protein, mouseMicrotubule-Associated Proteins

Identifiers

PMID21385839
PMCPMC3056604
OpenAlexW2102637166

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.