Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail
Beekman, J.M.; Bakema, J.E.; van der Poel, C.E.; van der Linden, J.A.; van de Winkel, J.G.J.; Leusen, J.H.W.
(2008) Molecular Immunology, volume 45, issue 7, pp. 2069 - 2075
(Article)
Abstract
The C-terminal domain of protein 4.1G was identified to interact with the cytosolic tail of the high affinity IgG receptor, Fc gamma RI, in yeast two-hybrid screens. Proteins of the 4.1 family have previously been found to mediate receptor/cytoskeleton interactions. In the study presented here, we show an alternatively spliced
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4.1G product to be associated with increased Fc gamma RI binding in yeast two-hybrid assays, and to be selectively enriched in most immune cells at the transcript level. In addition, a detailed analysis of the 4.1G 'docking site' within Fc gamma RI is provided by examining Fc gamma RI-CY-truncated and alanine-substituted mutants. These pointed to an Fc gamma RI membrane-proximal core motif of HxxBxxxBB (H represents hydrophobic residues, B basic residues and x represents any residue), followed by hydrophobic and (potentially) negatively charged residues to be central for interaction with protein 4.1G.
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Keywords: Alternative Splicing, Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Line, Cell Membrane, Cytoplasm, Cytoskeletal Proteins, Humans, Immunoprecipitation, Membrane Proteins, Mice, Molecular Sequence Data, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, RNA, Messenger, Receptors, IgG, Recombinant Proteins, Sequence Homology, Amino Acid, Two-Hybrid System Techniques, Journal Article, Research Support, Non-U.S. Gov't, Journal Article, Research Support, Non-U.S. Gov't
ISSN: 0161-5890
Publisher: Elsevier Limited
(Peer reviewed)
