Chaperone-directed ubiquitylation maintains proteostasis at the expense of longevity
نویسندگان
چکیده
منابع مشابه
Chaperone-directed ubiquitylation maintains proteostasis at the expense of longevity
The integrity of the cellular proteome is supported by quality control networks, which govern protein synthesis, folding, and degradation. It is generally accepted that an age-related decline in protein homeostasis (proteostasis) contributes to protein aggregation diseases. However, the mechanistic principles underlying proteostasis imbalance and the impact on life expectancy are not well under...
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Aging is modulated by environmental and physiological changes, involving genetic pathways that are conserved from yeast cells to mammalian organisms. Notably, Insulin/IGF-like signaling (IIS) contributes to the integrity of the cellular proteome and thus defines the aging process and the onset of age-related diseases. The insulin receptor named DAF-2 in C. elegans or INSR in mammals regulates f...
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A major challenge for metazoans is to ensure that different tissues, each expressing distinctive proteomes, are nevertheless well protected at an organismal level from proteotoxic stress. We show that expression of endogenous metastable proteins in muscle cells, which rely on chaperones for proper folding, induces a systemic stress response throughout multiple tissues of C. elegans. Suppression...
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Histone modifications play an important role in regulating access to DNA for transcription, DNA repair and DNA replication. A central player in these events is the mono-ubiquitylation of histone H2B (H2Bub1), which has been shown to regulate nucleosome dynamics. Previously, it was shown that H2Bub1 was important for nucleosome assembly onto nascent DNA at active replication forks. In the absenc...
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ژورنال
عنوان ژورنال: Worm
سال: 2017
ISSN: 2162-4054
DOI: 10.1080/21624054.2017.1371403