FcgammaRI depends for its biological function on both the intracellular domain of the alpha-chain and associated Fc receptor (FcR) gamma-chains. However, functional protein effectors of FcgammaRI's intracellular domain have not been identified. In this study, we identified periplakin (PPL) as a selective interacting protein for the intracellular tail of FcgammaRI but no other activatory FcRs. The interaction was confirmed by coimmunoprecipitation and blot-overlay assays. PPL and FcgammaRI colocalized at the plasma membrane in monocytes and cell transfectants, and both were up-regulated by IFN-gamma. By expressing C-terminal PPL in transfectants, we established a pivotal role for this protein in FcgammaRI ligand binding, endocytosis, and antigen presentation. These data illustrate that intracellular protein interactions with a multisubunit FcR alpha-chain can confer unique properties to the receptor.
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| rdf:type | |
| rdfs:comment |
FcgammaRI depends for its biological function on both the intracellular domain of the alpha-chain and associated Fc receptor (FcR) gamma-chains. However, functional protein effectors of FcgammaRI's intracellular domain have not been identified. In this study, we identified periplakin (PPL) as a selective interacting protein for the intracellular tail of FcgammaRI but no other activatory FcRs. The interaction was confirmed by coimmunoprecipitation and blot-overlay assays. PPL and FcgammaRI colocalized at the plasma membrane in monocytes and cell transfectants, and both were up-regulated by IFN-gamma. By expressing C-terminal PPL in transfectants, we established a pivotal role for this protein in FcgammaRI ligand binding, endocytosis, and antigen presentation. These data illustrate that intracellular protein interactions with a multisubunit FcR alpha-chain can confer unique properties to the receptor.
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| skos:exactMatch | |
| uniprot:name |
Proc. Natl. Acad. Sci. U.S.A.
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| uniprot:author |
Bakema J.E.,
Beekman J.M.,
Leusen J.H.W.,
van de Winkel J.G.J.
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| uniprot:date |
2004
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| uniprot:pages |
10392-10397
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| uniprot:title |
Direct interaction between FcgammaRI (CD64) and periplakin controls receptor endocytosis and ligand binding capacity.
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| uniprot:volume |
101
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| dc-term:identifier |
doi:10.1073/pnas.0401217101
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