Evidence map›Paper›PMID 25015291›Full record

ArticleJournal of cell science2014

Interaction of SQSTM1 with the motor protein dynein--SQSTM1 is required for normal dynein function and trafficking.

Luis Calderilla-Barbosa, M Lamar Seibenhener, Yifeng Du, Maria-Theresa Diaz-Meco, Jorge Moscat, Jin Yan, Marie W Wooten, Michael C Wooten

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

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  11. Review
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  15. The cytoplasmic dynein transport machinery and its many cargoes.Nature reviews. Molecular cell biology · 2018
    Review
  16. Article
  17. Development of Improved HDAC6 Inhibitors as Pharmacological Therapy for Axonal Charcot-Marie-Tooth Disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2017
    Article
  18. Article
  19. 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

8 authors at 3 institutions in 1 country.

Luis Calderilla-BarbosaDepartment of Biological Sciences, 331 Funchess Hall, Auburn University, Auburn, AL 36849, USA.
M Lamar SeibenhenerDepartment of Biological Sciences, 331 Funchess Hall, Auburn University, Auburn, AL 36849, USA.
Yifeng DuDepartment of Biological Sciences, 331 Funchess Hall, Auburn University, Auburn, AL 36849, USA.
Maria-Theresa Diaz-Meco10901 North Torrey Pines Road, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037, USA.
Jorge Moscat10901 North Torrey Pines Road, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037, USA.
Jin YanGraduate Center for Toxicology, Markey Cancer Center, University of Kentucky College of Medicine, Lexington, KY 40536, USA.
Marie W WootenDepartment of Biological Sciences, 331 Funchess Hall, Auburn University, Auburn, AL 36849, USA.
Michael C WootenDepartment of Biological Sciences, 331 Funchess Hall, Auburn University, Auburn, AL 36849, USA wootemc@auburn.edu.
Auburn University · USSanford Burnham Prebys Medical Discovery Institute · USThe Graduate Center, CUNY · US

Funding

NERVE GROWTH FACTOR SIGNALLINGR01NS033661 · NINDS · AUBURN UNIVERSITY AT AUBURN · PI WOOTEN, MICHAEL C · 1995 to 2013
$2.7M
NINDS NIH HHS 2R01NS033661NINDS NIH HHS R01 NS033661
6 · The paper itself

Abstract

The dynein motor protein complex is required for retrograde transport of vesicular cargo and for transport of aggregated proteins along microtubules for processing and degradation at perinuclear aggresomes. Disruption of this process leads to dysfunctional endosome accumulation and increased protein aggregation in the cell cytoplasm, both pathological features of neurodegenerative diseases. However, the exact mechanism of dynein functionality in these pathways is still being elucidated. Here, we show that the scaffolding protein SQSTM1 directly interacts with dynein through a previously unidentified dynein-binding site. This interaction is independent of HDAC6, a known interacting protein of both SQSTM1 and dynein. However, knockdown of HDAC6 increases the interaction of SQSTM1 with dynein, indicating a possible competitive interaction. Using different dynein cargoes, we show that SQSTM1 is required for proper dynein motility and trafficking along microtubules. Based on our results, we propose a new model of competitive interaction between SQSTM1 and HDAC6 with dynein. In this model, SQSTM1 would not only affect the association of polyubiquitylated protein aggregates and endosomes with dynein, but would also be required for normal dynein function.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCytoplasmic DyneinsEndosomesHeat-Shock ProteinsHistone Deacetylase 6Histone DeacetylasesHumansMiceMice, KnockoutMicrotubulesProtein BindingProtein Structure, TertiaryProtein TransportSequestosome-1 ProteinAdaptor Proteins, Signal TransducingCytoplasmic DyneinsDYNC1I1 protein, humanDync1li1 protein, mouseDYNC1LI2 protein, humanDYNC1LI2 protein, mouseHDAC6 protein, humanHeat-Shock ProteinsHistone Deacetylase 6Histone DeacetylasesSequestosome-1 ProteinSQSTM1 protein, humanSqstm1 protein, mouseAggresomeDynein intermediate chainHDAC6Histone deacetylase 6Late endosomeSQSTM1

Identifiers

PMID25015291
PMCPMC4163647
OpenAlexW2114716596

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.