Evidence map›Paper›PMID 30360468›Full record

ArticleMolecules (Basel, Switzerland)2018

The Two Isoforms of Lyn Display Different Intramolecular Fuzzy Complexes with the SH3 Domain.

João M C Teixeira, Héctor Fuentes, Stasė Bielskutė, Margarida Gairi, Szymon Żerko, Wiktor Koźmiński, Miquel Pons

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Review
  3. Dynamic regulatory features of the protein tyrosine kinases.Biochemical Society transactions · 2019
    Review
  4. Article
  5. Article
  6. 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

7 authors.

João M C TeixeiraBioNMR Laboratory, Inorganic and Organic Chemistry Department, University of Barcelona; Baldiri Reixac, 08028 Barcelona, Spain. joaomcteixeira@gmail.com.ORCID 0000-0002-9113-0622
Héctor FuentesBioNMR Laboratory, Inorganic and Organic Chemistry Department, University of Barcelona; Baldiri Reixac, 08028 Barcelona, Spain. hctr.fs@gmail.com.
Stasė BielskutėInstitute of Chemical Physics, Vilnius University, Saulétekio al.3, 10257 Vilnius, Lithuania. stase.bielskute@ff.vu.lt.
Margarida GairiLRB, Scientific and Technologic Centers of the University of Barcelona, Baldiri Reixac, 08028 Barcelona, Spain. mgairi@rmn.ub.edu.
Szymon ŻerkoFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw; Żwirki i Wigury 101, 02-089 Warsaw, Poland. szerko@chem.uw.edu.pl.ORCID 0000-0002-0044-1100
Wiktor KoźmińskiFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw; Żwirki i Wigury 101, 02-089 Warsaw, Poland. kozmin@chem.uw.edu.pl.ORCID 0000-0003-2319-4525
Miquel PonsBioNMR Laboratory, Inorganic and Organic Chemistry Department, University of Barcelona; Baldiri Reixac, 08028 Barcelona, Spain. mpons@ub.edu.

Funding

A NON INVASIVE DERMATOLOGICAL LESION CLASSIFIERR44CA078006 · NCI · WESTERN RESEARCH COMPANY, INC. · PI CRAINE, ERIC R. · 2000 to 2001
$722k
NONINVASIVE DERMATOLOGICAL LESION CLASSIFIERR43CA078006 · NCI · WESTERN RESEARCH COMPANY, INC. · PI CRAINE, ERIC R. · 1998 to 1998
–
Ministerio de Ciencia e Innovación BIO2016-78006RNarodowe Centrum Nauki MAESTRO Grant No. 2015/18/A/ST4/00270
6 · The paper itself

Abstract

The function of the intrinsically disordered Unique domain of the Src family of tyrosine kinases (SFK), where the largest differences between family members are concentrated, remains poorly understood. Recent studies in c-Src have demonstrated that the Unique region forms transient interactions, described as an intramolecular fuzzy complex, with the SH3 domain and suggested that similar complexes could be formed by other SFKs. Src and Lyn are members of a distinct subfamily of SFKs. Lyn is a key player in the immunologic response and exists in two isoforms originating from alternative splicing in the Unique domain. We have used NMR to compare the intramolecular interactions in the two isoforms and found that the alternatively spliced segment interacts specifically with the so-called RT-loop in the SH3 domain and that this interaction is abolished when a polyproline ligand binds to the SH3 domain. These results support the generality of the fuzzy complex formation in distinct subfamilies of SFKs and its physiological role, as the naturally occurring alternative splicing modulates the interactions in this complex.

Indexed as

Protein Interaction Domains and Motifssrc Homology DomainsAmino Acid SequenceHumansIsoenzymesMagnetic Resonance SpectroscopyModels, MolecularPeptidesProtein BindingProtein Conformationsrc-Family KinasesStructure-Activity RelationshipIsoenzymeslyn protein-tyrosine kinasePeptidespolyprolinesrc-Family KinasesFarseer-NMRfuzzy complexesintrinsically disordered proteinsLynnuclear magnetic resonanceSFKs unique domainsSH3 domainsSrcSrc family kinases

Identifiers

PMID30360468
PMCPMC6278449

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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.