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J. Biol. Chem., Vol. 276, Issue 14, 11174-11179, April 6, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/14/11174    most recent M010114200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gil, D. Articles by Alarcón, B. Search for Related Content PubMed PubMed Citation Articles by Gil, D. Articles by Alarcón, B. Social Bookmarking                      What's this?

Intracellular Redistribution of Nucleolin upon Interaction with the CD3 Chain of the T Cell Receptor Complex^*

Diana Gil, Dolores Gutiérrez, and Balbino Alarcón

From the Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Cantoblanco, Madrid 28049, Spain

T cell activation through the antigen receptor (TCR) involves the cytoplasmic tails of the CD3 subunits CD3, CD3, CD3, and CD3. Whereas the biological significance of the cytoplasmic tails of these molecules is suggested, in part, by their evolutionarily conserved sequences, their interactions with signal transduction molecules are not completely understood. We used affinity chromatography columns of glutathione S-transferase fused to the CD3 cytoplasmic tail to isolate proteins that specifically interact with this subunit. In this way, we identified the shuttling protein nucleolin as a specific CD3-interacting molecule. Using competition studies and affinity chromatography on peptide columns, we were able to identify a central proline-rich sequence as the nucleolin-interacting sequence in CD3. Transfection in COS cells of wild type CD3, but not of nonbinding mutants of CD3, resulted in redistribution of nucleolin from the nucleus and nucleoli to the cytoplasm. This property was transferred to a CD8 protein chimera by appending the cytoplasmic tail of CD3. We also found that nucleolin associated with the TCR complex. This association was increased upon TCR engagement, suggesting that the CD3/nucleolin interaction may have a role in T cell activation.

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