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.

doi:https://doi.org/10.1016/j.molimm.2007.10.024

Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail

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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 ... read more

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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

DOI: https://doi.org/10.1016/j.molimm.2007.10.024

ISSN: 0161-5890

Publisher: Elsevier Limited

(Peer reviewed)

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