A sequence conserved between CD5 and CD6 binds an FERM domain and exerts a restraint on T-cell activation.


Journal

Immunology
ISSN: 1365-2567
Titre abrégé: Immunology
Pays: England
ID NLM: 0374672

Informations de publication

Date de publication:
03 2019
Historique:
received: 22 10 2018
accepted: 14 11 2018
pubmed: 22 11 2018
medline: 30 8 2019
entrez: 22 11 2018
Statut: ppublish

Résumé

CD5 and CD6 are related surface receptors that limit and promote T-cell responses. Co-stimulatory effects of CD6 depend on binding a cell surface ligand, CD166, and recruitment of the intracellular adaptor proteins GADS and SLP-76 by C-terminal phosphotyrosines. We have continued to identify interactions of CD5 and CD6 to understand their roles in T-cell activation. In a screen to identify binding partners for peptides containing a cytoplasmic sequence, SDSDY conserved between CD5 and CD6, we identified ezrin radixin moesin (ERM) proteins, which link plasma membrane proteins to actin. Purified radixin FERM domain bound directly to CD5 and CD6 SDSDY peptides in a phosphorylation-dependent manner (K

Identifiants

pubmed: 30460991
doi: 10.1111/imm.13025
pmc: PMC6376265
doi:

Substances chimiques

Actins 0
Antibodies, Monoclonal 0
Antigens, CD 0
Antigens, Differentiation, T-Lymphocyte 0
CD5 Antigens 0
CD6 antigen 0
DNA-Binding Proteins 0
Tyrosine 42HK56048U

Banques de données

GENBANK
['NP_001093259', 'HSU34623']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

270-276

Subventions

Organisme : Medical Research Council
ID : G0400808
Pays : United Kingdom

Informations de copyright

© 2018 The Authors. Immunology Published by John Wiley & Sons Ltd.

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Auteurs

Johannes Breuning (J)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Marion H Brown (MH)

Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

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Classifications MeSH