Shaping proteostasis at the cellular, tissue, and organismal level.
TLDR
This review by Morimoto and colleagues examines mechanisms by which protein homeostasis (proteostasis) is achieved in multicellular organisms and discusses the implications for health and disease.Abstract:
The proteostasis network (PN) regulates protein synthesis, folding, transport, and degradation to maintain proteome integrity and limit the accumulation of protein aggregates, a hallmark of aging and degenerative diseases. In multicellular organisms, the PN is regulated at the cellular, tissue, and systemic level to ensure organismal health and longevity. Here we review these three layers of PN regulation and examine how they collectively maintain cellular homeostasis, achieve cell type-specific proteomes, and coordinate proteostasis across tissues. A precise understanding of these layers of control has important implications for organismal health and could offer new therapeutic approaches for neurodegenerative diseases and other chronic disorders related to PN dysfunction.read more
Citations
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Book ChapterDOI
Proteome-scale studies of protein stability
Giulia Calloni,R. Martin Vabulas +1 more
TL;DR: The proteomic studies of protein stability have significant novelty potential in basic and applied biomedical research and several important areas of their application have ensured an increasing interest and significant advances in the respective MS-based approaches.
Journal ArticleDOI
HLH-1 Modulates Muscle Proteostasis During Caenorhabditis elegans Larval Development
Khairun Nisaa,Anat Ben-Zvi +1 more
TL;DR: It is proposed that the differentiation transcription factor, HLH-1, contributes to muscle maintenance and regulates cell-specific chaperone expression post differentiation and may impact muscle proteostasis and potentially the onset and manifestation of sarcopenia.
Journal ArticleDOI
Differential contributions of the proteasome, autophagy, and chaperones to the clearance of arsenite-induced protein aggregates in yeast
Sansan Hua,Agnieszka Kłosowska,Joana Isabel Rodrigues,Gabriel Petelski,L. A. Esquembre,Emma Lorentzon,Lars Folke Olsen,Krzysztof Liberek,Markus J. Tamás +8 more
TL;DR: In this article , the authors systematically assessed the contribution of the ubiquitin-proteasome system, the autophagy-vacuole pathway, and chaperone-mediated disaggregation to the clearance of arsenite-induced protein aggregates in Saccharomyces cerevisiae.
Journal ArticleDOI
Molecular regulation, breed differences and genes involved in stress control in farm animals.
TL;DR: In this article , a review examined molecular regulation, breed differences, and genes involved in stress control in farm animals, such as oxidative, cytosolic heat shock, unfolded protein, and hypoxic responses, were discussed.
Posted ContentDOI
Hsp47 Promotes Biogenesis of Multi-subunit Neuroreceptors in the Endoplasmic Reticulum
Yajuan Wang,Xiaojing Di,Dong-Yun Han,Raad Nashmi,Brandon J. Henderson,Fraser J. Moss,Ting Wei Mu +6 more
TL;DR: In this paper , a heat shock protein, called SERPINH1, was identified as a chaperone for gamma-aminobutyric type A (GABAA) receptor functional surface expression, acting after Binding immunoglobulin Protein (BiP) to preferentially bind the folded conformation of GABAA receptors.
References
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Tissue-based map of the human proteome
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The Ubiquitin System
Avram Hershko,Aaron Ciechanover +1 more
TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
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The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Peter Walter,David Ron +1 more
TL;DR: The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum, where they fold and assemble, and only properly assembled proteins advance from the ER to the cell surface.
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An nrf2/small maf heterodimer mediates the induction of phase ii detoxifying enzyme genes through antioxidant response elements
Ken Itoh,Tomoki Chiba,Satoru Takahashi,Tetsuro Ishii,Kazuhiko Igarashi,Yasutake Katoh,Tatsuya Oyake,Norio Hayashi,Kimihiko Satoh,Ichiro Hatayama,Masayuki Yamamoto,Yo-ichi Nabeshima +11 more
TL;DR: It is demonstrated that Nrf2 is essential for the transcriptional induction of phase II enzymes and the presence of a coordinate transcriptional regulatory mechanism for phase II enzyme genes and the nrf2-deficient mice may prove to be a very useful model for the in vivo analysis of chemical carcinogenesis and resistance to anti-cancer drugs.
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Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy
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TL;DR: Two genes encode ubiquitin ligases that are potential drug targets for the treatment of muscle atrophy, and mice deficient in either MAFbx orMuRF1 were found to be resistant to atrophy.