Protein interactions: anything new?

被引：10
作者：
Barrera-Vilarmau, Susana [1 ]
Teixeira, Joao M. C. [1 ]
Fuxreiter, Monika [1 ,2 ]
机构：
[1] Univ Padua, Dept Biomed Sci, Padua, Italy
[2] Univ Padua, Dept Phys & Astron, Padua, Italy
来源：
ESSAYS IN BIOCHEMISTRY | 2022年 / 66卷 / 07期
关键词：
ETS-1; DNA-BINDING; PHASE-SEPARATION; ENERGY LANDSCAPES; HELICAL STRUCTURE; FUZZY COMPLEXES; P53; FRUSTRATION; MUTATIONS; DYNAMICS; DISORDER;
D O I：
10.1042/EBC20220044
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：
How do proteins interact in the cellular environment? Which interactions stabilize liquid-liquid phase separated condensates? Are the concepts, which have been developed for specific protein complexes also applicable to higher-order assemblies? Recent discov-eries prompt for a universal framework for protein interactions, which can be applied across the scales of protein communities. Here, we discuss how our views on protein interactions have evolved from rigid structures to conformational ensembles of proteins and discuss the open problems, in particular related to biomolecular condensates. Protein interactions have evolved to follow changes in the cellular environment, which manifests in multiple modes of interactions between the same partners. Such cellular context-dependence requires multi-plicity of binding modes (MBM) by sampling multiple minima of the interaction energy land-scape. We demonstrate that the energy landscape framework of protein folding can be ap-plied to explain this phenomenon, opening a perspective toward a physics-based, universal model for cellular protein behaviors.
引用
收藏
页码：821 / 830
页数：10
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