mTORC1 Links Protein Quality and Quantity Control by Sensing Chaperone Availability
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TLDR
It is demonstrated that cells distinguish moderate reductions in protein quality from severe protein misfolding using molecular chaperones to differentially regulate mTORC1 signaling, and the tight linkage between protein quality and quantity control provides a plausible mechanism coupling protein mis folding with metabolic dyshomeostasis.About:
This article is published in Journal of Biological Chemistry.The article was published on 2010-08-27 and is currently open access. It has received 50 citations till now. The article focuses on the topics: Hsp33 & Chaperone (protein).read more
Citations
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Modulation of apolipoprotein b-100 degradation and secretion by hepatic protein quality control components
TL;DR: Data suggest that ubiquitination is the committing step in the apoB-100 ERAD pathway and that ubiquitate may play a regulatory role in VLDL assembly, and that the loss of Bag6 function increased the degradation of apo B-100.
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PDIA3 Expression Is Altered in the Limbic Brain Regions of Triple-Transgenic Mouse Model of Alzheimer’s Disease
Tommaso Cassano,Flavia Giamogante,Silvio Calcagnini,Adele Romano,Angelo Michele Lavecchia,Francesca Inglese,Giuliano Paglia,Vidyasagar Naik Bukke,Antonino Romano,Marzia Friuli,Fabio Altieri,Silvana Gaetani +11 more
TL;DR: In this paper , a mouse model of Alzheimer's disease (AD) (3×Tg-AD mice) was used to longitudinally analyse the expression level of PDIA3, a protein disulfide isomerase and endoplasmic reticulum (ER) chaperone, in selected brain limbic areas strongly affected by AD-pathology.
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TORC1 regulates autophagy induction in response to proteotoxic stress in yeast and human cells.
Kazuki Suda,Atsuki Kaneko,Mitsugu Shimobayashi,Akio Nakashima,Tatsuya Maeda,Michael N. Hall,Takashi Ushimaru +6 more
TL;DR: It is shown that proteotoxic stress after treatment with azetidine-2-carboxylic acid (AZC), a toxic proline analog, induces autophagy in budding yeast, and suggested that TORC1 is a conserved key factor to cope with proteot toxic stress in eukaryotic cells.
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Proteostatic Signaling & Control of Protein Synthesis
TL;DR: This review examines the critical neuronal signaling networks employed to control translation with an emphasis on current research, including the Unfolded Protein Response (UPR), the mitochondrial UPR, mTORC1 signaling, and stress granule formation.
References
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Journal ArticleDOI
TOR signaling in growth and metabolism.
TL;DR: The physiological consequences of mammalianTORC1 dysregulation suggest that inhibitors of mammalian TOR may be useful in the treatment of cancer, cardiovascular disease, autoimmunity, and metabolic disorders.
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Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
David E. Harrison,Randy Strong,Zelton D Sharp,James F. Nelson,Clinton M. Astle,Kevin Flurkey,Nancy L. Nadon,J. Erby Wilkinson,Krystyna Frenkel,Christy S. Carter,Christy S. Carter,Marco Pahor,Marco Pahor,Martin A. Javors,Elizabeth Fernandez,Richard A. Miller +15 more
TL;DR: It is reported that rapamycin, an inhibitor of the mTOR pathway, extends median and maximal lifespan of both male and female mice when fed beginning at 600 days of age.
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mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery
Do Hyung Kim,Dos D. Sarbassov,Siraj M. Ali,Jessie E. King,Robert R. Latek,Hediye Erdjument-Bromage,Paul Tempst,David M. Sabatini +7 more
TL;DR: It is reported that mTOR forms a stoichiometric complex with raptor, an evolutionarily conserved protein with at least two roles in the mTOR pathway that through its association with mTOR regulates cell size in response to nutrient levels.
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TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
TL;DR: It is shown that TSC1–TSC2 inhibits the p70 ribosomal protein S6 kinase 1 and activates the eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translational initiation) and these functions are mediated by inhibition of the mammalian target of rapamycin (mTOR).
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Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton.
Dos D. Sarbassov,Siraj M. Ali,Do Hyung Kim,David A. Guertin,Robert R. Latek,Hediye Erdjument-Bromage,Paul Tempst,David M. Sabatini +7 more
TL;DR: It is found that the rictor-mTOR complex modulates the phosphorylation of Protein Kinase C alpha (PKCalpha) and the actin cytoskeleton, suggesting that this aspect of TOR signaling is conserved between yeast and mammals.