Evidence map›Paper›PMID 23394833›Full record

ArticleCurrent biology : CB2013

The microtubule-binding protein ensconsin is an essential cofactor of kinesin-1.

Kari Barlan, Wen Lu, Vladimir I Gelfand

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

85 citing papers in PubMed, 151 citations in OpenAlex.

  1. Article
  2. PolyQ-Expansion of Ataxin-2 Disrupts Microtubule Stability and Impairs Axon Outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  3. Review
  4. Article
  5. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
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  7. Article
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  11. Article
  12. Article
  13. Review
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  17. Article
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  20. Article

25 more citing papers are in PubMed but not listed here.

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.

Kari BarlanDepartment of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Wen Lu
Vladimir I Gelfand
Northwestern University · US

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
REGULATION OF MYOSIN DRIVEN ORGANELLE TRANSPORTR01GM052111 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GELFAND, VLADIMIR I · 1999 to 2018
$8.3M
NIGMS NIH HHS R01 GM052111NIGMS NIH HHS R01GM052111NIGMS NIH HHS T32 GM008061NIGMS NIH HHS T32 GM08061
6 · The paper itself

Abstract

Kinesin-1 is a major microtubule motor that drives transport of numerous cellular cargoes toward the plus ends of microtubules. In the cell, kinesin-1 exists primarily in an inactive, autoinhibited state, and motor activation is thought to occur upon binding to cargo through the C terminus. Using RNAi-mediated depletion in Drosophila S2 cells, we demonstrate that kinesin-1 requires ensconsin (MAP7, E-MAP-115), a ubiquitous microtubule-associated protein, for its primary function of organelle transport. We show that ensconsin is required for organelle transport in Drosophila neurons and that Drosophila homozygous for ensconsin gene deletion are unable to survive to adulthood. An ensconsin N-terminal truncation that cannot bind microtubules is sufficient to activate organelle transport by kinesin-1, indicating that this activating domain functions independently of microtubule binding. Interestingly, ens mutant flies retaining expression of this truncation show normal viability. A "hingeless" mutant of kinesin-1, which mimics the active conformation of the motor, does not require ensconsin for transport in S2 cells, suggesting that ensconsin plays a role in relieving autoinhibition of kinesin-1. Together with other recent work, our study suggests that ensconsin is an essential cofactor for all known functions of kinesin-1.

Indexed as

AnimalsCell LineDrosophilaDrosophila ProteinsGene DeletionGreen Fluorescent ProteinsKinesinsMicrotubule-Associated ProteinsMicrotubulesMutationProtein BindingProtein TransportRecombinant Fusion ProteinsRNA InterferenceRNA, Small InterferingDrosophila ProteinsGreen Fluorescent ProteinsKhc protein, DrosophilaKinesinsMicrotubule-Associated ProteinsRecombinant Fusion ProteinsRNA, Small Interfering

Identifiers

PMID23394833
PMCPMC3580027
OpenAlexW2019578272

What OpenQuestion holds

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LicenceTDM
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.