Evidence map›Paper›PMID 30690395›Full record

ArticleiScience2019

A Myristoyl-Binding Site in the SH3 Domain Modulates c-Src Membrane Anchoring.

Anabel-Lise Le Roux, Irrem-Laareb Mohammad, Borja Mateos, Miguel Arbesú, Margarida Gairí, Farman Ali Khan, João M C Teixeira, Miquel Pons

Abstract read
In one paragraph

Article in iScience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
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  9. Article
  10. Review
  11. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Nuclear Functions of the Tyrosine Kinase Src.International journal of molecular sciences · 2020
    Review
  17. Article
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.

Anabel-Lise Le RouxBioNMR Laboratory, Inorganic and Organic Chemistry Department, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain.
Irrem-Laareb MohammadBioNMR Laboratory, Inorganic and Organic Chemistry Department, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain.
Borja MateosBioNMR Laboratory, Inorganic and Organic Chemistry Department, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain.
Miguel ArbesúBioNMR Laboratory, Inorganic and Organic Chemistry Department, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain.
Margarida GairíNMR Facility, Scientific and Technological Centers, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain.
Farman Ali KhanBioNMR Laboratory, Inorganic and Organic Chemistry Department, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain; Department of Biochemistry, Abdul Wali Khan University, Mardan 23200, Pakistan.
João M C TeixeiraBioNMR Laboratory, Inorganic and Organic Chemistry Department, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain.
Miquel PonsBioNMR Laboratory, Inorganic and Organic Chemistry Department, Universitat de Barcelona, Baldiri Reixac, 10-12, 08028 Barcelona, Spain. Electronic address: mpons@ub.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The c-Src oncogene is anchored to the cytoplasmic membrane through its N-terminal myristoylated SH4 domain. This domain is part of an intramolecular fuzzy complex with the SH3 and Unique domains. Here we show that the N-terminal myristoyl group binds to the SH3 domain in the proximity of the RT loop, when Src is not anchored to a lipid membrane. Residues in the so-called Unique Lipid Binding Region modulate this interaction. In the presence of lipids, the myristoyl group is released from the SH3 domain and inserts into the lipid membrane. The fuzzy complex with the SH4 and Unique domains is retained in the membrane-bound form, placing the SH3 domain close to the membrane surface and restricting its orientation. The apparent affinity of myristoylated proteins containing the SH4, Unique, and SH3 domains is modulated by these intramolecular interactions, suggesting a mechanism linking c-Src activation and membrane anchoring.

Indexed as

BiophysicsProtein Structure AspectsStructural Biology

Identifiers

PMID30690395
PMCPMC6354742

What OpenQuestion holds

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Registered trials

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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.