Discovering immunoreceptor coupling and organization motifs

被引:2
|
作者
Reth, Michael [1 ,2 ]
机构
[1] Univ Freiburg, Fac Biol, Dept Mol Immunol, Biol 3, Freiburg, Germany
[2] Univ Freiburg, Signaling Res Ctr CIBSS & BIOSS, Freiburg, Germany
来源
FRONTIERS IN IMMUNOLOGY | 2023年 / 14卷
基金
美国国家卫生研究院;
关键词
antigen receptors; ITAM; nanoscale receptor organization; leucine zipper; resting state of lymphocytes; CELL ANTIGEN RECEPTOR; PDGF-BETA-RECEPTOR; CRYO-EM STRUCTURE; ERYTHROPOIETIN RECEPTOR; TRANSMEMBRANE DOMAIN; ACTIVATION; PROTEIN; COMPLEX; RP105; CD45;
D O I
10.3389/fimmu.2023.1253412
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The recently determined cryo-EM structures of the T cell antigen receptor (TCR) and B cell antigen receptor (BCR) show in molecular details the interactions of the ligand-binding part with the signaling subunits but they do not reveal the signaling mechanism of these antigen receptors. Without knowing the molecular basis of antigen sensing by these receptors, a rational design of optimal vaccines is not possible. The existence of conserved amino acids (AAs) that are not involved in the subunit interaction suggests that antigen receptors form higher complexes and/or have lateral interactors that control their activity. Here, I describe evolutionary conserved leucine zipper (LZ) motifs within the transmembrane domains (TMD) of antigen and coreceptor components that are likely to be involved in the oligomerization and lateral interaction of antigen receptor complexes on T and B cells. These immunoreceptor coupling and organization motifs (ICOMs) are also found within the TMDs of other important receptor types and viral envelope proteins. This discovery suggests that antigen receptors do not function as isolated entities but rather as part of an ICOM-based interactome that controls their nanoscale organization on resting cells and their dynamic remodeling on activated lymphocytes.
引用
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页数:11
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