SRC homology 3 domains: multifaceted binding modules

被引:20
作者
Dionne, Ugo [1 ,2 ,3 ,8 ]
Percival, Lily J. [1 ,2 ,3 ]
Chartier, Francois J. M. [1 ,2 ,3 ]
Landry, Christian R. [2 ,3 ,4 ,5 ,6 ]
Bisson, Nicolas [1 ,2 ,3 ,7 ]
机构
[1] Univ Laval, Ctr Rech Canc, Ctr Rech CHU Quebec, Quebec City, PQ, Canada
[2] Univ Manchester, Fac Biol Med & Hlth, Sch Biol Sci, Michael Smith Bldg, Manchester, England
[3] Quebec Network Res Prot Funct Engn & Applicat PROT, Quebec City, PQ, Canada
[4] Univ Laval, Inst Integrat & Syst Biol, Quebec City, PQ, Canada
[5] Univ Laval, Dept Biochem Microbiol & Bioinformat, Quebec City, PQ, Canada
[6] Univ Laval, Dept Biol, Quebec City, PQ, Canada
[7] Univ Laval, Departmen Mol Biol Med Biochem & Pathol, Quebec City, PQ, Canada
[8] Lunenfeld Tanenbaum Res Inst, Sinai Hlth, Toronto, ON, Canada
基金
加拿大健康研究院; 加拿大自然科学与工程研究理事会;
关键词
PROTEIN-INTERACTION NETWORKS; SH3; DOMAIN; TYROSINE PHOSPHORYLATION; SUPERTERTIARY STRUCTURE; PEPTIDE-RECOGNITION; PHASE-TRANSITION; MOLECULAR-BASIS; LIGAND-BINDING; FAMILY; SPECIFICITY;
D O I
10.1016/j.tibs.2022.04.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The assembly of complexes following the detection of extracellular signals is often controlled by signaling proteins comprising multiple peptide binding modules. The SRC homology (SH)3 family represents the archetypical modular protein interaction module, with similar to 300 annotated SH3 domains in humans that regulate an impressive array of signaling processes. We review recent findings regarding the allosteric contributions of SH3 domains host protein context, their phosphoregulation, and their roles in phase separation that challenge the simple model in which SH3s are considered to be portable domains binding to specific proline-rich peptide motifs.
引用
收藏
页码:772 / 784
页数:13
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