The famous British developmental biologist Waddington proposed the concept of“Canalization”in 1942[1],which generalized the robustness of living systems in the face of internal gene mutation and external environment...The famous British developmental biologist Waddington proposed the concept of“Canalization”in 1942[1],which generalized the robustness of living systems in the face of internal gene mutation and external environmental stress,it can buffer various endogenous and exogenous perturbations and maintain the homeostasis of the phenotype.For an extended period,this phenomenon has been overlooked as mere genetic redundancy within the field of biomolecular genetics research,and the underlying molecular mechanisms have largely remained uninvestigated.Developmental robustness is a core characteristic of organisms that respond to extreme environmental stress.One such mechanism is the protein-folding chaperone,the heat shock protein 90(Hsp90),which helps to protect against cellular stress.Hsp90 is an ATP-dependent protein folding chaperone that protects intracellular protein homeostasis,buffers perturbations during protein folding,alleviates the effects of harmful mutations,and conceals certain mutant phenotypes.However,this buffering capacity may be compromised by protein-toxic stressors,and Hsp90 mutations could either enhance or diminish genetic canalization in a genotype-dependent manner.Recently,the research team led by Georgios Ioannis Karras at the University of Texas recently published a breakthrough study in the journal Science,which focused on and analyzed the mechanism of Hsp90 in the biological canalization process[2](Fig.1).展开更多
基金supported by National Natural Science Foundation of China(32170084)Natural Science Foundation of Shandong Province(ZR2023MC163)National Key R&D Program of China(2022YFC2106200).
文摘The famous British developmental biologist Waddington proposed the concept of“Canalization”in 1942[1],which generalized the robustness of living systems in the face of internal gene mutation and external environmental stress,it can buffer various endogenous and exogenous perturbations and maintain the homeostasis of the phenotype.For an extended period,this phenomenon has been overlooked as mere genetic redundancy within the field of biomolecular genetics research,and the underlying molecular mechanisms have largely remained uninvestigated.Developmental robustness is a core characteristic of organisms that respond to extreme environmental stress.One such mechanism is the protein-folding chaperone,the heat shock protein 90(Hsp90),which helps to protect against cellular stress.Hsp90 is an ATP-dependent protein folding chaperone that protects intracellular protein homeostasis,buffers perturbations during protein folding,alleviates the effects of harmful mutations,and conceals certain mutant phenotypes.However,this buffering capacity may be compromised by protein-toxic stressors,and Hsp90 mutations could either enhance or diminish genetic canalization in a genotype-dependent manner.Recently,the research team led by Georgios Ioannis Karras at the University of Texas recently published a breakthrough study in the journal Science,which focused on and analyzed the mechanism of Hsp90 in the biological canalization process[2](Fig.1).
