Su Ting-Yi, Xia Yu
Graduate Program in Quantitative Life Sciences, McGill University, Montréal, Québec, Canada.
Department of Bioengineering, McGill University, Montréal, Québec, Canada.
Protein Sci. 2025 Jun;34(6):e70155. doi: 10.1002/pro.70155.
The complex genotype-to-phenotype relationships in Mendelian diseases can be elucidated by mutation-induced disturbances to the networks of molecular interactions (interactomes) in human cells. Missense and nonsense mutations cause distinct perturbations within the human protein interactome, leading to functional and phenotypic effects with varying degrees of severity. Here, we structurally resolve the human protein interactome at atomic-level resolutions and perform structural and thermodynamic calculations to assess the biophysical implications of these mutations. We focus on a specific type of missense mutation, known as "quasi-null" mutations, which destabilize proteins and cause similar functional consequences (node removal) to nonsense mutations. We propose a "fold difference" quantification of deleteriousness, which measures the ratio between the fractions of node-removal mutations in datasets of Mendelian disease-causing and non-pathogenic mutations. We estimate the fold differences of node-removal mutations to range from 3 (for quasi-null mutations with folding ΔΔG ≥2 kcal/mol) to 20 (for nonsense mutations). We observe a strong positive correlation between biophysical destabilization and phenotypic deleteriousness, demonstrating that the deleteriousness of quasi-null mutations spans a continuous spectrum, with nonsense mutations at the extreme (highly deleterious) end. Our findings substantiate the disparity in phenotypic severity between missense and nonsense mutations and suggest that mutation-induced protein destabilization is indicative of the phenotypic outcomes of missense mutations. Our analyses of node-removal mutations allow for the potential identification of proteins whose removal or destabilization lead to harmful phenotypes, enabling the development of targeted therapeutic approaches, and enhancing comprehension of the intricate mechanisms governing genotype-to-phenotype relationships in clinically relevant diseases.
孟德尔疾病中复杂的基因型与表型关系可通过突变对人类细胞中分子相互作用网络(互作组)的干扰来阐明。错义突变和无义突变会在人类蛋白质互作组中引起不同的扰动,导致严重程度不同的功能和表型效应。在此,我们以原子水平分辨率解析人类蛋白质互作组,并进行结构和热力学计算,以评估这些突变的生物物理影响。我们聚焦于一种特定类型的错义突变,即“准无效”突变,它会使蛋白质不稳定,并导致与无义突变类似的功能后果(节点去除)。我们提出一种“折叠差异”有害性量化方法,该方法测量孟德尔致病突变和非致病突变数据集中节点去除突变比例之间的比率。我们估计节点去除突变的折叠差异范围为3(对于折叠ΔΔG≥2千卡/摩尔的准无效突变)至20(对于无义突变)。我们观察到生物物理不稳定与表型有害性之间存在很强的正相关,这表明准无效突变的有害性跨越一个连续谱,无义突变处于极端(高度有害)端。我们的研究结果证实了错义突变和无义突变在表型严重程度上的差异,并表明突变引起的蛋白质不稳定指示了错义突变的表型结果。我们对节点去除突变的分析有助于潜在识别那些去除或不稳定会导致有害表型的蛋白质,从而能够开发靶向治疗方法,并增强对临床相关疾病中基因型与表型关系复杂机制的理解。