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<dc:title>CD229 (Ly9) lymphocyte cell surface receptor Interacts homophilically through Its N-Terminal domain and relocalizes to the immunological synapse</dc:title>
<dc:creator>Romero, Xavier</dc:creator>
<dc:creator>Zapater, Nuria</dc:creator>
<dc:creator>Calvo, María</dc:creator>
<dc:creator>Kalko, Susana G.</dc:creator>
<dc:creator>Fuente García, Miguel Ángel de la</dc:creator>
<dc:creator>Tovar, Victoria</dc:creator>
<dc:creator>Ockeloen, Charlotte</dc:creator>
<dc:creator>Pizcueta, Pilar</dc:creator>
<dc:creator>Engel, Pablo</dc:creator>
<dc:subject>Inmunología</dc:subject>
<dc:description>Producción Científica</dc:description>
<dc:description>CD229 is a member of the CD150 family of the Ig superfamily expressed on T and B cells. Receptors of this family regulate&#xd;
cytokine production and cytotoxicity of lymphocytes and NK cells. The cytoplasmic tail of CD229 binds to SAP, a protein that is&#xd;
defective in X-linked lymphoproliferative syndrome. To identify the CD229 ligand, we generated a soluble Ig fusion protein&#xd;
containing the two N-terminal extracellular domains of human CD229 (CD229-Ig). CD229-Ig bound to CD229-transfected cells,&#xd;
whereas no binding was detected on cells expressing other CD150 family receptors, showing that CD229 binds homophilically.&#xd;
Both human and mouse CD229 interacted with itself. Domain deletion mutants showed that the N-terminal Ig-domain mediates&#xd;
homophilic adhesion. CD229-CD229 binding was severely compromised when the charged amino acids E27 and E29 on the&#xd;
predicted B-C loop and R89 on the F-G loop of the N-terminal domain were mutated to alanine. In contrast, one mutation, R44A,&#xd;
enhanced the homophilic interaction. Confocal microscopy image analysis revealed relocalization of CD229 to the contact area of&#xd;
T and B cells during Ag-dependent immune synapse formation. Thus, CD229 is its own ligand and participates in the immunological&#xd;
synapse.</dc:description>
<dc:date>2015-03-26T09:14:22Z</dc:date>
<dc:date>2015-03-26T09:14:22Z</dc:date>
<dc:date>2005</dc:date>
<dc:type>info:eu-repo/semantics/article</dc:type>
<dc:identifier>The Journal of Immunology, 2005, vol. 174, n. 11. p. 7033–7042.</dc:identifier>
<dc:identifier>0022-1767</dc:identifier>
<dc:identifier>http://uvadoc.uva.es/handle/10324/10117</dc:identifier>
<dc:identifier>10.4049/jimmunol.174.11.7033</dc:identifier>
<dc:identifier>7033</dc:identifier>
<dc:identifier>11</dc:identifier>
<dc:identifier>7042</dc:identifier>
<dc:identifier>The Journal of Immunology</dc:identifier>
<dc:identifier>174</dc:identifier>
<dc:language>eng</dc:language>
<dc:relation>https://www.jimmunol.org/content/174/11/7033</dc:relation>
<dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
<dc:rights>http://creativecommons.org/licenses/by-nc-nd/4.0/</dc:rights>
<dc:rights>Attribution-NonCommercial-NoDerivatives 4.0 International</dc:rights>
<dc:publisher>American Association of Immunologists</dc:publisher>
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