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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.

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IMMUNOBIOLOGY

Dendritic cells regulate T-cell deattachment through the integrin-interacting protein CYTIP

Susanne Hofer, Karina Pfeil, Harald Niederegger, Susanne Ebner, Van Anh Nguyen, Elisabeth Kremmer, Margit Auffinger, Susanne Neyer, Christina Fürhapter, and Christine Heufler

From the Department of Dermatology, Medical University of Innsbruck, Innsbruck, Austria; the Department of Pathophysiology, Medical University of Innsbruck, Innsbruck, Austria; and the GSF-National Research Center for Environment and Health, Munich, Germany.

When T cells are primed by dendritic cells (DCs) 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. Although 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 deattachment. CYTIP, which is induced during maturation of DCs, shortly accumulates to the contact zones with T cells within the first hour of coculture. Specific silencing of CYTIP results in stronger adhesion of DCs to T cells and to fibronectin. When a need for deattachment is created in a T-cell priming assay by only partially loading DCs with antigen, CYTIP silencing causes reduced priming capacity. Thus, CYTIP allows DCs to actively control DC-T-cell interactions.


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