Faulty proteins
Proteins are the workhorses of the cell, and their function depends on their shape.
When proteins are misfolded or damaged, their shape becomes flawed and they can’t perform their duties. Faulty proteins need to be eliminated before they accumulate, clump or become toxic. Although there are intrinsic cell mechanisms that recognize defective proteins and attempt to remove them, these systems go awry as we age. Almost every age-related degenerative disease is linked to protein misfolding.
Director's statement
Our focus is on understanding how cells discriminate between functional and nonfunctional proteins. We have made important discoveries about the damaging impact of oxidative stress on protein structure and function in the neurodegenerative diseases of Alzheimer’s and Parkinson’s, metabolic diseases of diabetes and liver failure, and inflammatory disease and cancer. Our findings will be translated into new therapies that improve protein folding and preserve cell function in diseases that are major worldwide health concerns.
– Randal J. Kaufman, Ph.D., Program Director
Appointments
Program Director
Primary Appointments
Secondary Appointments
Publications
Chop/Ddit3 depletion in β cells alleviates ER stress and corrects hepatic steatosis in mice.
Yong J, Parekh VS, Reilly SM, Nayak J, Chen Z, Lebeaupin C, Jang I, Zhang J, Prakash TP, Sun H, Murray S, Guo S, Ayala JE, Satin LS, Saltiel AR, Kaufman RJ
Sci Transl Med 2021 Jul 28 ;13(604)
Trem2 deletion enhances tau dispersion and pathology through microglia exosomes.
Zhu B, Liu Y, Hwang S, Archuleta K, Huang H, Campos A, Murad R, Piña-Crespo J, Xu H, Huang TY
Mol Neurodegener 2022 Sep 2 ;17(1):58
Somatic APP gene recombination in Alzheimer's disease and normal neurons.
Lee MH, Siddoway B, Kaeser GE, Segota I, Rivera R, Romanow WJ, Liu CS, Park C, Kennedy G, Long T, Chun J
Nature 2018 Nov ;563(7733):639-645
