Recognition sequences for the GYF domain reveal a possible spliceosomal function of CD2BP2.

Protein Engineering Group, Forschungsinstitut fuer Molekulare Pharmakologie und Freie Universitaet Berlin, Robert-Roessle-Strasse 10, 13125 Berlin, Germany.
Protein-protein interactions are often mediated by small domains that recognize solvent-exposed peptide sequences. Deciphering the recognition code for these adapter domains is an important step in the understanding of multi-protein assemblies. Here, we investigate the sequence requirements for the CD2BP2-GYF domain, a proline-rich sequence binding module previously shown to be involved in T cell signaling. We show that the signature (R/K/G)XXPPGX(R/K) defines a preferred peptide-binding motif that is present in several proteins of the splicing machinery. Specifically, the core small nuclear ribonucleoprotein, SmB/B', contains several PPP-PGMR motifs that interact with the CD2BP2-GYF domain in vitro and in vivo. The colocalization of CD2BP2 and SmB proteins in the nucleus of Jurkat T cells and HeLa cells suggests a function of the GYF domain of CD2BP2 in mediating protein-protein interactions within the spliceosome.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Alternative Splicing, Amino Acid Motifs, Amino Acid Sequence, Autoantigens, Carrier Proteins, Cell Membrane, Databases as Topic, Glutathione Transferase, Glycine, Green Fluorescent Proteins, HeLa Cells, Humans, Jurkat Cells, Kinetics, Ligands, Luminescent Proteins, Magnetic Resonance Spectroscopy, Microscopy, Fluorescence, Molecular Sequence Data, Peptides, Proline, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Ribonucleoproteins, Small Nuclear, Signal Transduction, Software, Spliceosomes, Transfection, snRNP Core Proteins
J. Biol. Chem. Jul. 02, 2004; 279(27);28292-7 [PUBMED:15105431]
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