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Blood, 1 February 2006, Vol. 107, No. 3, pp. 1003-1009. Prepublished online as a Blood First Edition Paper on October 4, 2005; DOI 10.1182/blood-2005-01-0425. This Article Full Text (PDF) All Versions of this Article: 2005-01-0425v1 107/3/1003    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Hofer, S. Articles by Heufler, C. Search for Related Content PubMed PubMed Citation Articles by Hofer, S. Articles by Heufler, C. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted January 31, 2005 Accepted September 20, 2005 Dendritic cells regulate T-cell de-attachment through the integrin-interacting protein CYTIP Susanne Hofer, Karina Pfeil, Harald Niederegger, Susanne Ebner, Van Anh Nguyen, Elisabeth Kremmer, Margit Auffinger, Susanne Neyer, Christina Furhapter, and Christine Heufler* Dept. of Dermatology, Medical University of Innsbruck, Innsbruck, Austria Dept. of Pathophysiology, Medical University of Innsbruck, Innsbruck, Austria GSF-National Research Center for Environment and Health, Munich, Germany * Corresponding author; email: Christine.Heufler{at}uibk.ac.at. When T-cells are primed by dendritic cells (DC) to initiate antigen-specific immune responses screening for matching antigen receptor-MHC/peptide pairs takes place in DC-T-cell conjugates. For an immune response DC-T-cell conjugates formed during priming events need to dissolve. While detailed knowledge on molecules involved in the conjugate formation is available, dissolving of them has not been considered to be an active process. Here we identify CYTIP (cytohesin-interacting protein) to mediate DC-T-cell de-attachment. CYTIP, which is induced during maturation of DC, shortly accumulates to the contact zones with T-cells within the first hour of co-culture. Specific silencing of CYTIP results in stronger adhesion of DC to T-cells and to fibronectin. When a need for de-attachment is created in a T-cell priming assay by only partially loading DC with antigen, CYTIP silencing causes reduced priming capacity . Thus, CYTIP allows DC to actively control DC-T-cell interactions. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: V. Coppola, C. A. Barrick, S. Bobisse, M. C. Rodriguez-Galan, M. Pivetta, D. Reynolds, O. M. Z. Howard, M. E. Palko, P. F. Esteban, H. A. Young, et al. The scaffold protein cybr is required for cytokine-modulated trafficking of leukocytes in vivo. Mol. Cell. Biol., July 1, 2006; 26(14): 5249 - 5258. [Abstract] [Full Text] [PDF]

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