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Vav1 dephosphorylation by the tyrosine phosphatase SHP-1 as a mechanism for inhibition of cellular cytotoxicity

Here, we present data suggesting a novel mechanism for regulation of natural killer (NK) cell cytotoxicity through inhibitory receptors. Interaction of activation receptors with their ligands on target cells induces cytotoxicity by NK cells. This activation is under negative control by inhibitory re...

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Main Authors: Stebbins, Christopher (Author) , Watzl, Carsten (Author) , Billadeau, Daniel D. (Author) , Leibson, Paul J. (Author) , Burshtyn, Deborah N. (Author) , Long, Eric O. (Author)
Format: Article (Journal)
Language:English
Published: 2003
In: Molecular and cellular biology
Year: 2003, Volume: 23, Issue: 17, Pages: 6291-6299
ISSN:1098-5549
DOI:10.1128/mcb.23.17.6291-6299.2003
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1128/mcb.23.17.6291-6299.2003
Verlag, lizenzpflichtig, Volltext: https://mcb.asm.org/content/23/17/6291
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Author Notes:Christopher C. Stebbins, Carsten Watzl, Daniel D. Billadeau, Paul J. Leibson, Deborah N. Burshtyn, and Eric O. Long

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520 |a Here, we present data suggesting a novel mechanism for regulation of natural killer (NK) cell cytotoxicity through inhibitory receptors. Interaction of activation receptors with their ligands on target cells induces cytotoxicity by NK cells. This activation is under negative control by inhibitory receptors that recruit tyrosine phosphatase SHP-1 upon binding major histocompatibility class I on target cells. How SHP-1 blocks the activation pathway is not known. To identify SHP-1 substrates, an HLA-C-specific inhibitory receptor fused to a substrate-trapping mutant of SHP-1 was expressed in NK cells. Phosphorylated Vav1, a regulator of actin cytoskeleton, was the only protein detectably associated with the catalytic site of SHP-1 during NK cell contact with target cells expressing HLA-C. Vav1 trapping was independent of actin polymerization, suggesting that inhibition of cellular cytotoxicity occurs through an early dephosphorylation of Vav1 by SHP-1, which blocks actin-dependent activation signals. Such a mechanism explains how inhibitory receptors can block activating signals induced by different receptors. 
650 4 |a Actins 
650 4 |a Binding, Competitive 
650 4 |a Catalytic Domain 
650 4 |a Cell Cycle Proteins 
650 4 |a Cells, Cultured 
650 4 |a Cytoskeleton 
650 4 |a Cytotoxicity Tests, Immunologic 
650 4 |a Cytotoxicity, Immunologic 
650 4 |a HLA-C Antigens 
650 4 |a Humans 
650 4 |a Intracellular Signaling Peptides and Proteins 
650 4 |a Killer Cells, Natural 
650 4 |a Mutation 
650 4 |a Phosphorylation 
650 4 |a Protein Tyrosine Phosphatase, Non-Receptor Type 6 
650 4 |a Protein Tyrosine Phosphatases 
650 4 |a Proto-Oncogene Proteins 
650 4 |a Proto-Oncogene Proteins c-vav 
650 4 |a Receptors, Immunologic 
650 4 |a Receptors, KIR 
650 4 |a Recombinant Fusion Proteins 
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