Comparison of the peptide binding preferences of three closely related TRAF paralogs: TRAF2, TRAF3, and TRAF5

Protein Science : a Publication of the Protein Society
Glenna Wink Foight, Amy E Keating

Abstract

Tumor necrosis factor receptor-associated factors (TRAFs) constitute a family of adapter proteins that act in numerous signaling pathways important in human biology and disease. The MATH domain of TRAF proteins binds peptides found in the cytoplasmic domains of signaling receptors, thereby connecting extracellular signals to downstream effectors. Beyond several very general motifs, the peptide binding preferences of TRAFs have not been extensively characterized, and differences between the binding preferences of TRAF paralogs are poorly understood. Here we report a screening system that we established to explore TRAF peptide-binding specificity using deep mutational scanning of TRAF-peptide ligands. We displayed single- and double-mutant peptide libraries based on the TRAF-binding sites of CD40 or TANK on the surface of Escherichia coli and screened them for binding to TRAF2, TRAF3, and TRAF5. Enrichment analysis of the library sequencing results showed differences in the permitted substitution patterns in the TANK versus CD40 backgrounds. The three TRAF proteins also demonstrated different preferences for binding to members of the CD40 library, and three peptides from that library that were analyzed individually showed strikin...Continue Reading

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Citations

Nov 2, 2019·The Journal of Immunology : Official Journal of the American Association of Immunologists·Sabyasachi DasMasayuki Hirano
Mar 13, 2018·Current Pharmacology Reports·Almin I LalaniPing Xie
Dec 14, 2018·Frontiers in Immunology·Juan M ZapataIgnacio Melero
Sep 15, 2018·Frontiers in Immunology·Hyun H Park
Apr 25, 2020·International Journal of Molecular Sciences·Chang Min Kim, Hyun Ho Park
Nov 24, 2020·Frontiers in Cell and Developmental Biology·Wei ZhouQifa Ye
Jun 2, 2021·Fish & Shellfish Immunology·Mengshi SunJingguang Wei

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