Modulation of FcγRI (CD64) ligand binding by blocking peptides of periplakin

Jeffrey M. Beekman, Jantine E. Bakema, Joke Van Der Linden, Bastiaan Tops, Marja Hinten, Martine Van Vugt, Jan G.J. Van De Winkel, Jeanette H.W. Leusen

Onderzoeksoutput: Bijdrage aan tijdschriftArtikelpeer review

24 Citaten (Scopus)

Samenvatting

FcγRI requires both the intracellular domain of the α-chain and associated leukocyte Fc receptor (FcR) γ-chains for its biological function. We recently found the C terminus of periplakin to selectively interact with the cytoplasmic domain of the FcγRI α-chain. It thereby enhances the capacity of FcγRI to bind, internalize, and present antigens on MHC class II. Here, we characterized the domains involved in FcγRI-periplakin interaction using truncated and alanine-substituted FcγRI mutants and randomly mutagenized periplakin. This allowed us to design TAT peptides that selectively interfered with endogenous FcγRI-periplakin interactions. The addition of these peptides to FcγRI-expressing cells modulated FcγRI ligand binding, as assessed by erythrocyte-antibody-rosetting. These data support a dominant-negative role of C-terminal periplakin for FcγRI biological activity and implicate periplakin as a novel regulator of FcγRI in immune cells.

Originele taal-2Engels
Pagina's (van-tot)33875-33881
Aantal pagina's7
TijdschriftJournal of Biological Chemistry
Volume279
Nummer van het tijdschrift32
DOI's
StatusGepubliceerd - 6 aug. 2004
Extern gepubliceerdJa

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