Evidence map›Paper›PMID 21949238›Full record

ArticleThe Journal of biological chemistry2011

Binding to syntenin-1 protein defines a new mode of ubiquitin-based interactions regulated by phosphorylation.

Sundaresan Rajesh, Ružica Bago, Elena Odintsova, Gayrat Muratov, Gouri Baldwin, Pooja Sridhar, Sandya Rajesh, Michael Overduin, Fedor Berditchevski

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Guideline
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  11. A molecular perspective of mammalian autophagosome biogenesis.The Journal of biological chemistry · 2018
    Review
  12. Article
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  17. Autophagy signal transduction by ATG proteins: from hierarchies to networks.Cellular and molecular life sciences : CMLS · 2015
    Review
  18. Targeting tumor invasion: the roles of MDA-9/Syntenin.Expert opinion on therapeutic targets · 2015
    Review
  19. Article
  20. Review
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

9 authors at 1 institution in 1 country.

Sundaresan RajeshSchool of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Ružica Bago
Elena Odintsova
Gayrat Muratov
Gouri Baldwin
Pooja Sridhar
Sandya Rajesh
Michael Overduin
Fedor Berditchevski
University of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research CouncilBreast Cancer Now 2008NOVPR52Cancer Research UK
6 · The paper itself

Abstract

Syntenin-1 is a PDZ domain-containing adaptor that controls trafficking of transmembrane proteins including those associated with tetraspanin-enriched microdomains. We describe the interaction of syntenin-1 with ubiquitin through a novel binding site spanning the C terminus of ubiquitin, centered on Arg(72), Leu(73), and Arg(74). A conserved LYPSL sequence in the N terminus, as well as the C-terminal region of syntenin-1, are essential for binding to ubiquitin. We present evidence for the regulation of this interaction through syntenin-1 dimerization. We have also established that syntenin-1 is phosphorylated downstream of Ulk1, a serine/threonine kinase that plays a critical role in autophagy and regulates endocytic trafficking. Importantly, Ulk1-dependent phosphorylation of Ser(6) in the LYPSL prevents the interaction of syntenin-1 with ubiquitin. These results define an unprecedented ubiquitin-dependent pathway involving syntenin-1 that is regulated by Ulk1.

Indexed as

Amino Acid MotifsAutophagyAutophagy-Related Protein-1 HomologBinding SitesBiological Transport, ActiveEndocytosisHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsPhosphorylationProtein BindingProtein MultimerizationProtein Serine-Threonine KinasesProtein Structure, TertiarySynteninsAutophagy-Related Protein-1 HomologIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesSDCBP protein, humanSynteninsUbiquitinULK1 protein, human

Identifiers

PMID21949238
PMCPMC3234783
OpenAlexW2044802039

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.