Evidence map›Paper›PMID 25944905›Full record

ArticleThe Journal of biological chemistry2015

JIP3 Activates Kinesin-1 Motility to Promote Axon Elongation.

Dana Watt, Ram Dixit, Valeria Cavalli

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
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  9. Selective motor activation in organelle transport along axons.Nature reviews. Molecular cell biology · 2022
    Review
  10. Article
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  15. 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

3 authors at 1 institution in 1 country.

Dana WattDepartment of Anatomy and Neurobiology, School of Medicine, Washington University, St. Louis, Missouri 63110.
Ram DixitDepartment of Biology, Washington University, St. Louis, Missouri 63110.
Valeria CavalliDepartment of Anatomy and Neurobiology, School of Medicine, Washington University, St. Louis, Missouri 63110. Electronic address: cavalli@pcg.wustl.edu.
Washington University in St. Louis · US

Funding

Systems and Molecular Neurobiology Training ProgramT32GM008151 · NIGMS · WASHINGTON UNIVERSITY · PI SNYDER, LAWRENCE H · 1985 to 2019
$6.5M
MICROTUBULE POST-TRANSLATIONAL MODIFICATIONS IN AXON REGENERATIONR01NS082446 · NINDS · WASHINGTON UNIVERSITY · PI CAVALLI, VALERIA · 2013 to 2017
$1.7M
NIGMS NIH HHS T32 GM008151NINDS NIH HHS R01 NS082446
6 · The paper itself

Abstract

Kinesin-1 is a molecular motor responsible for cargo transport along microtubules and plays critical roles in polarized cells, such as neurons. Kinesin-1 can function as a dimer of two kinesin heavy chains (KHC), which harbor the motor domain, or as a tetramer in combination with two accessory light chains (KLC). To ensure proper cargo distribution, kinesin-1 activity is precisely regulated. Both KLC and KHC subunits bind cargoes or regulatory proteins to engage the motor for movement along microtubules. We previously showed that the scaffolding protein JIP3 interacts directly with KHC in addition to its interaction with KLC and positively regulates dimeric KHC motility. Here we determined the stoichiometry of JIP3-KHC complexes and observed approximately four JIP3 molecules binding per KHC dimer. We then determined whether JIP3 activates tetrameric kinesin-1 motility. Using an in vitro motility assay, we show that JIP3 binding to KLC engages kinesin-1 with microtubules and that JIP3 binding to KHC promotes kinesin-1 motility along microtubules. We tested the in vivo relevance of these findings using axon elongation as a model for kinesin-1-dependent cellular function. We demonstrate that JIP3 binding to KHC, but not KLC, is essential for axon elongation in hippocampal neurons as well as axon regeneration in sensory neurons. These findings reveal that JIP3 regulation of kinesin-1 motility is critical for axon elongation and regeneration.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsAxonsHEK293 CellsHippocampusHumansKinesinsMiceMicrotubulesMultiprotein ComplexesNerve Tissue ProteinsProtein MultimerizationProtein TransportSensory Receptor CellsAdaptor Proteins, Signal TransducingKinesinsMapk8ip3 protein, mouseMultiprotein ComplexesNerve Tissue ProteinsaxonJIP3KHCkinesinmolecular motormotilityneurite outgrowthregeneration

Identifiers

PMID25944905
PMCPMC4505465
OpenAlexW2224873906

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.