Evidence map›Paper›PMID 21390300›Full record

ArticlePLoS biology2011

A role for myosin VI in the localization of axonal proteins.

Tommy L Lewis, Tianyi Mao, Don B Arnold

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  7. Optogenetics at the presynapse.Nature neuroscience · 2022
    Review
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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 2 institutions in 1 country.

Tommy L LewisDepartment of Biological Sciences, University of Southern California, Los Angeles, California, United States of America.
Tianyi Mao
Don B Arnold
University of Southern California · USHoward Hughes Medical Institute · US

Funding

Subcellular Localization of Neuronal Ion ChannelsR01NS041963 · NINDS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI ARNOLD, DONALD B · 2002 to 2013
$3.6M
Subcellular targeting of light-responsive opsins for mapping and manipulating neuR01MH086381 · NIMH · UNIVERSITY OF SOUTHERN CALIFORNIA · PI ARNOLD, DONALD B · 2009 to 2013
$2.0M
Subcellular Localization of Neuronal Ion ChannelsK02MH071439 · NIMH · UNIVERSITY OF SOUTHERN CALIFORNIA · PI ARNOLD, DONALD B · 2004 to 2008
$610k
LKB1 function in axon development through regulation of mitochondrial traffickingF32NS080464 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI LEWIS, TOMMY L · 2012 to 2014
$156k
NIMH NIH HHS K02 MH071439NIMH NIH HHS MH-071439NIMH NIH HHS R01 MH086381NINDS NIH HHS F32 NS080464NINDS NIH HHS NS-041963NINDS NIH HHS R01 NS041963
6 · The paper itself

Abstract

In neurons polarized trafficking of vesicle-bound membrane proteins gives rise to the distinct molecular composition and functional properties of axons and dendrites. Despite their central role in shaping neuronal form and function, surprisingly little is known about the molecular processes that mediate polarized targeting of neuronal proteins. Recently, the plus-end-directed motor Myosin Va was shown to play a critical role in targeting of transmembrane proteins to dendrites; however, the role of myosin motors in axonal targeting is unknown. Here we show that Myosin VI, a minus-end-directed motor, plays a vital role in the enrichment of proteins on the surface of axons. Engineering non-neuronal proteins to interact with Myosin VI causes them to become highly concentrated at the axonal surface in dissociated rat cortical neurons. Furthermore, disruption of either Myosin VI function or expression leads to aberrant dendritic localization of axonal proteins. Myosin VI mediates the enrichment of proteins on the axonal surface at least in part by stimulating dendrite-specific endocytosis, a mechanism that has been shown to underlie the localization of many axonal proteins. In addition, a version of Channelrhodopsin 2 that was engineered to bind to Myosin VI is concentrated at the surface of the axon of cortical neurons in mice in vivo, suggesting that it could be a useful tool for probing circuit structure and function. Together, our results indicate that myosins help shape the polarized distributions of both axonal and dendritic proteins.

Indexed as

AnimalsAxonsChannelrhodopsinsChlorocebus aethiopsCOS CellsDNA, ComplementaryElectrophysiologyEndocytosisImmunohistochemistryImmunoprecipitationLuminescent ProteinsMembrane ProteinsMiceMyosin Heavy ChainsNerve Tissue ProteinsProtein TransportChannelrhodopsinsDNA, ComplementaryLuminescent ProteinsMembrane ProteinsMyosin Heavy Chainsmyosin VINerve Tissue ProteinsRNA, Small Interfering

Identifiers

PMID21390300
PMCPMC3046960
OpenAlexW2053457621

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.