Evidence map›Paper›PMID 28775156›Full record

ArticleJournal of cell science2017

The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex.

Meraj H Khan, Siiri I Salomaa, Guillaume Jacquemet, Umar Butt, Mitro Miihkinen, Takahiro Deguchi, Elena Kremneva, Pekka Lappalainen, Martin J Humphries, Jeroen Pouwels

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Review
  3. SHARPIN stabilizes β-catenin through a linear ubiquitination-independent manner to support gastric tumorigenesis.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2021
    Article
  4. Article
  5. TheScience signaling · 2020
    Article
  6. Article
  7. SHARPIN at the nexus of integrin, immune, and inflammatory signaling in human platelets.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Meraj H KhanTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku 20520, Finland.
Siiri I SalomaaTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku 20520, Finland.
Guillaume JacquemetTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku 20520, Finland.
Umar ButtTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku 20520, Finland.
Mitro MiihkinenTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku 20520, Finland.
Takahiro DeguchiTurku Doctoral Programme of Molecular Medicine, University of Turku, Turku 20520, Finland.
Elena KremnevaInstitute of Biotechnology, University of Helsinki, Helsinki 00790, Finland.
Pekka LappalainenInstitute of Biotechnology, University of Helsinki, Helsinki 00790, Finland.
Martin J HumphriesWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.
Jeroen PouwelsTurku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku 20520, Finland jerpou@utu.fi.ORCID http://orcid.org/0000-0002-5388-6103
Åbo Akademi University · FIUniversity of Helsinki · FIUniversity of Turku · FIWellcome Centre for Cell-Matrix Research · GB

Funding

Cancer Research UK 21671Wellcome Trust 092015
6 · The paper itself

Abstract

Sharpin, a multifunctional adaptor protein, regulates several signalling pathways. For example, Sharpin enhances signal-induced NF-κB signalling as part of the linear ubiquitin assembly complex (LUBAC) and inhibits integrins, the T cell receptor, caspase 1 and PTEN. However, despite recent insights into Sharpin and LUBAC function, a systematic approach to identify the signalling pathways regulated by Sharpin has not been reported. Here, we present the first 'Sharpin interactome', which identifies a large number of novel potential Sharpin interactors in addition to several known ones. These data suggest that Sharpin and LUBAC might regulate a larger number of biological processes than previously identified, such as endosomal trafficking, RNA processing, metabolism and cytoskeleton regulation. Importantly, using the Sharpin interactome, we have identified a novel role for Sharpin in lamellipodium formation. We demonstrate that Sharpin interacts with Arp2/3, a protein complex that catalyses actin filament branching. We have identified the Arp2/3-binding site in Sharpin and demonstrate using a specific Arp2/3-binding deficient mutant that the Sharpin-Arp2/3 interaction promotes lamellipodium formation in a LUBAC-independent fashion.This article has an associated First Person interview with the first author of the paper.

Indexed as

Protein Interaction MapsActin-Related Protein 2-3 ComplexCell MovementCytoskeletonGene OntologyHeLa CellsHumansMass SpectrometryNerve Tissue ProteinsProtein BindingPseudopodiaTime-Lapse ImagingActin-Related Protein 2-3 ComplexNerve Tissue ProteinssharpinArp2/3InteractomeLinear ubiquitylationLUBACSharpin

Identifiers

PMID28775156
PMCPMC5612173
OpenAlexW2744896017

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.