Regulation of organismal mitochondrial proteostasis in C. elegans
Xueying Wu1, #, Qian Zhang1,2, #, Peng Chen1,2,, Limeng Liu1, Nan Xin3, Ye Tian1,*, Andrew Dillin3,* 1State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China; 2Graduate School, University of Chinese Academy of Sciences, Beijing 100093, China; 3Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA; The Paul F. Glenn Center for Aging Research, University of California, Berkeley, Berkeley, CA 94720, USA Correspondence: firstname.lastname@example.org and email@example.com
The mitochondrial unfolded protein response (UPRmt) can be triggered in a cell-non-autonomous fashion across multiple tissues in response to mitochondrial dysfunction. The ability to communicate information about the presence of mitochondrial stress enables a global response that can ultimately better protect an animal from locally sensed stresses. Studies in C. elegans have established that the expression of the polyQ40 protein in neurons initiates the UPRmt in the intestine, a process that induces global alteration of transcription networks to maintain a functional mitochondrial proteome. These studies have led to the concept of a “mitokine”— a signal generated in cells experiencing mitochondrial stress that is secreted, propagated, and subsequently perceived by peripheral tissues to regulate mitochondrial proteostasis. In an attempt to identify a mitokine signal, we characterized EMS mutants that are defective in cell-non-autonomous UPRmt signaling. The characterizations of these mutants will allow us to understand the molecular nature of mitokine signaling.
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