Journal article
Transmembrane features governing Fc receptor CD16A assembly with CD16A signaling adaptor molecules
A Blázquez-Moreno, S Park, W Im, MJ Call, ME Call, HT Reyburn
Proceedings of the National Academy of Sciences of the United States of America | NATL ACAD SCIENCES | Published : 2017
Abstract
Many activating immunoreceptors associate with signaling adaptor molecules like FcϵR1γ or CD247. FcϵR1γ and CD247 share high sequence homology and form disulphide-linked homodimers that contain a pair of acidic aspartic acid residues in their transmembrane (TM) domains that mediate assembly, via interaction with an arginine residue at a similar register to these aspartic acids, with the activating immunoreceptors. However, this model cannot hold true for receptors like CD16A, whose TM domains do not contain basic residues. We have carried out an extensive site-directed mutagenesis analysis of the CD16A receptor complex and now report that the association of receptor with the signaling adapto..
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Awarded by National Institute of General Medical Sciences
Funding Acknowledgements
We thank Dr. Cesar Santiago for helpful advice on design of the mutagenesis strategy; Dr. Mar Vales Gomez for critical reading of the manuscript; Ruth Lopez-Caro, Dr. Mario Mellado, Pilar Lucas, Dr. Laura Martinez-Munoz, and Dr. Blanca Soler-Palacios for constructive advice and help; and Dr. Gloria Esteso for daily encouragement and support. This work was supported by Ministerio de Economia y Competitividad (MINECO) Grant SAF2014-58752-R (to H.T.R.), MINECO PhD Studentship SVP-2014-068263 (to A. B.-M.), Australian Research Council Future Fellowship FT120100145 (to M.J.C.), Extreme Science and Engineering Discovery Environment Grant MCB070009 (to W.I.), National Science Foundation Grant MCB-1727508 (to W.I.), and National Institutes of Health Grant R01-GM092950 (to W.I.).