Source:http://linkedlifedata.com/resource/pubmed/id/19654330
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
40
|
| pubmed:dateCreated |
2009-10-5
|
| pubmed:abstractText |
The killer cell lectin-like receptor G1, KLRG1, is a cell surface receptor expressed on subsets of natural killer (NK) cells and T cells. KLRG1 was recently found to recognize E-cadherin and thus inhibit immune responses by regulating the effector function and the developmental processes of NK and T cells. E-cadherin is expressed on epithelial cells and exhibits Ca(2+)-dependent homophilic interactions that contribute to cell-cell junctions. However, the mechanism underlying the molecular recognition of KLRG1 by E-cadherin remains unclear. Here, we report structural, binding, and functional analyses of this interaction using multiple methods. Surface plasmon resonance demonstrated that KLRG1 binds the E-cadherin N-terminal domains 1 and 2 with low affinity (K(d) approximately 7-12 microm), typical of cell-cell recognition receptors. NMR binding studies showed that only a limited N-terminal region of E-cadherin, comprising the homodimer interface, exhibited spectrum perturbation upon KLRG1 complex formation. It was confirmed by binding studies using a series of E-cadherin mutants. Furthermore, killing assays using KLRG1(+)NK cells and reporter cell assays demonstrated the functional significance of the N-terminal region of E-cadherin. These results suggest that KLRG1 recognizes the N-terminal homodimeric interface of domain 1 of E-cadherin and binds only the monomeric form of E-cadherin to inhibit the immune response. This raises the possibility that KLRG1 detects monomeric E-cadherin at exposed cell surfaces to control the activation threshold of NK and T cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
1083-351X
|
| pubmed:author |
pubmed-author:IkuraMitsuhikoM,
pubmed-author:ItoMasayukiM,
pubmed-author:KajikawaMizuhoM,
pubmed-author:KamedaYosukeY,
pubmed-author:KurokiKimikoK,
pubmed-author:MaenakaKatsumiK,
pubmed-author:MaruyamaTakumaT,
pubmed-author:MatsumotoNaokiN,
pubmed-author:NakamuraSeikoS,
pubmed-author:OhkiIzuruI,
pubmed-author:SasakiKaoriK,
pubmed-author:YamamotoKazuoK
|
| pubmed:issnType |
Electronic
|
| pubmed:day |
2
|
| pubmed:volume |
284
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
27327-35
|
| pubmed:dateRevised |
2010-10-5
|
| pubmed:meshHeading |
pubmed-meshheading:19654330-Amino Acid Sequence,
pubmed-meshheading:19654330-Animals,
pubmed-meshheading:19654330-Binding Sites,
pubmed-meshheading:19654330-Cadherins,
pubmed-meshheading:19654330-Cattle,
pubmed-meshheading:19654330-Cell Line, Tumor,
pubmed-meshheading:19654330-Gene Expression Regulation,
pubmed-meshheading:19654330-Killer Cells, Natural,
pubmed-meshheading:19654330-Magnetic Resonance Spectroscopy,
pubmed-meshheading:19654330-Mice,
pubmed-meshheading:19654330-Models, Molecular,
pubmed-meshheading:19654330-Molecular Sequence Data,
pubmed-meshheading:19654330-Mutagenesis,
pubmed-meshheading:19654330-Protein Binding,
pubmed-meshheading:19654330-Protein Multimerization,
pubmed-meshheading:19654330-Protein Structure, Quaternary,
pubmed-meshheading:19654330-Protein Structure, Tertiary,
pubmed-meshheading:19654330-Receptors, Immunologic,
pubmed-meshheading:19654330-Recombinant Proteins,
pubmed-meshheading:19654330-Staining and Labeling,
pubmed-meshheading:19654330-Surface Plasmon Resonance
|
| pubmed:year |
2009
|
| pubmed:articleTitle |
Molecular basis for E-cadherin recognition by killer cell lectin-like receptor G1 (KLRG1).
|
| pubmed:affiliation |
Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|