Document Detail


Non-catalytic tyrosine-phosphorylated receptors.
MedLine Citation:
PMID:  23046135     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Leukocytes play a critical role in recognizing and responding to infection and cancer. Central to this function is an array of cell-surface receptors that lack sequence homology. Many of these receptors have in common the fact that their signaling involves phosphorylation of cytoplasmic domains by extrinsic tyrosine kinases. These non-catalytic tyrosine-phosphorylated receptors (NTRs) share a number of other features, including small size and optimal stimulation by surface-associated ligands. We argue here that NTRs are also likely to share the same kinetic-segregation triggering mechanism, which involves segregation of the engaged NTR from receptor tyrosine phosphatases with large ectodomains such as CD45 and CD148. NTRs signal through tyrosine-containing cytoplasmic motifs, which recruit distinct cytoplasmic signaling proteins when phosphorylated, transducing activatory or inhibitory signals. They have two features that make them uniquely well suited to their role in immune recognition of infection and cancer. Their modular structure enables the coupling of many rapidly evolving receptors with diverse ligand specificities to the same conserved signaling machinery. Their similarity in size and shared signaling machinery enables them to colocalize at cell-cell interfaces when they engage ligands, facilitating the integration of activatory and inhibitory signals from multiple receptors at the cell surface.
Authors:
Omer Dushek; Jesse Goyette; P Anton van der Merwe
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Immunological reviews     Volume:  250     ISSN:  1600-065X     ISO Abbreviation:  Immunol. Rev.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-10-10     Completed Date:  2013-02-25     Revised Date:  2014-02-20    
Medline Journal Info:
Nlm Unique ID:  7702118     Medline TA:  Immunol Rev     Country:  England    
Other Details:
Languages:  eng     Pagination:  258-76     Citation Subset:  IM    
Copyright Information:
© 2012 John Wiley & Sons A/S.
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MeSH Terms
Descriptor/Qualifier:
Humans
Immunity, Innate*
Immunologic Surveillance
Leukocytes / immunology*,  metabolism
Ligands
Phosphorylation
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Protein Tyrosine Phosphatases / immunology*,  metabolism
Protein-Tyrosine Kinases / metabolism
Receptors, Cell Surface / immunology*,  metabolism
Signal Transduction / immunology*
Grant Support
ID/Acronym/Agency:
G19/31//Medical Research Council; G9722488//Medical Research Council; MR/J002011/1//Medical Research Council
Chemical
Reg. No./Substance:
0/Ligands; 0/Receptors, Cell Surface; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 3.1.3.48/Protein Tyrosine Phosphatases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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