Database : MEDLINE
Search on : Proteostasis and Deficiencies [Words]
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[PMID]: 28459531
[Au] Autor:Troilo F; Bonetti D; Toto A; Visconti L; Brunori M; Longhi S; Gianni S
[Ad] Address:Istituto Pasteur - Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli" and Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Università di Roma , 00185, Rome, Italy.
[Ti] Title:The Folding Pathway of the KIX Domain.
[So] Source:ACS Chem Biol;12(6):1683-1690, 2017 06 16.
[Is] ISSN:1554-8937
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The KIX domain is an 89-residues globular domain with an important role in mediating protein-protein interactions. The presence of two distinct binding sites in such a small domain makes KIX a suitable candidate to investigate the effect of the potentially divergent demands between folding and function. Here, we report an extensive mutational analysis of the folding pathway of the KIX domain, based on 30 site-directed mutants, which allow us to assess the structures of both the transition and denatured states. Data reveal that, while the transition state presents mostly native-like interactions, the denatured state is somewhat misfolded. We mapped some of the non-native contacts in the denatured state using a second round of mutagenesis, based on double mutant cycles on 15 double mutants. Interestingly, such a misfolding arises from non-native interactions involving the residues critical for the function of the protein. The results described in this work appear to highlight the diverging demands between folding and function that may lead to misfolding, which may be observed in the early stages of folding.
[Mh] MeSH terms primary: Metabolic Networks and Pathways
Protein Folding
[Mh] MeSH terms secundary: Binding Sites/genetics
Humans
Mutagenesis, Site-Directed
Protein Denaturation
Protein Domains/genetics
Protein Domains/physiology
Proteostasis Deficiencies/genetics
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Entry month:1709
[Cu] Class update date: 180201
[Lr] Last revision date:180201
[Js] Journal subset:IM
[Da] Date of entry for processing:170502
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00289

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[PMID]: 29293508
[Au] Autor:Hadizadeh Esfahani A; Sverchkova A; Saez-Rodriguez J; Schuppert AA; Brehme M
[Ad] Address:Joint Research Center for Computational Biomedicine (JRC-COMBINE), RWTH Aachen University, Aachen, Germany.
[Ti] Title:A systematic atlas of chaperome deregulation topologies across the human cancer landscape.
[So] Source:PLoS Comput Biol;14(1):e1005890, 2018 01.
[Is] ISSN:1553-7358
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Proteome balance is safeguarded by the proteostasis network (PN), an intricately regulated network of conserved processes that evolved to maintain native function of the diverse ensemble of protein species, ensuring cellular and organismal health. Proteostasis imbalances and collapse are implicated in a spectrum of human diseases, from neurodegeneration to cancer. The characteristics of PN disease alterations however have not been assessed in a systematic way. Since the chaperome is among the central components of the PN, we focused on the chaperome in our study by utilizing a curated functional ontology of the human chaperome that we connect in a high-confidence physical protein-protein interaction network. Challenged by the lack of a systems-level understanding of proteostasis alterations in the heterogeneous spectrum of human cancers, we assessed gene expression across more than 10,000 patient biopsies covering 22 solid cancers. We derived a novel customized Meta-PCA dimension reduction approach yielding M-scores as quantitative indicators of disease expression changes to condense the complexity of cancer transcriptomics datasets into quantitative functional network topographies. We confirm upregulation of the HSP90 family and also highlight HSP60s, Prefoldins, HSP100s, ER- and mitochondria-specific chaperones as pan-cancer enriched. Our analysis also reveals a surprisingly consistent strong downregulation of small heat shock proteins (sHSPs) and we stratify two cancer groups based on the preferential upregulation of ATP-dependent chaperones. Strikingly, our analyses highlight similarities between stem cell and cancer proteostasis, and diametrically opposed chaperome deregulation between cancers and neurodegenerative diseases. We developed a web-based Proteostasis Profiler tool (Pro2) enabling intuitive analysis and visual exploration of proteostasis disease alterations using gene expression data. Our study showcases a comprehensive profiling of chaperome shifts in human cancers and sets the stage for a systematic global analysis of PN alterations across the human diseasome towards novel hypotheses for therapeutic network re-adjustment in proteostasis disorders.
[Mh] MeSH terms primary: Molecular Chaperones/metabolism
Neoplasms/metabolism
Proteostasis
[Mh] MeSH terms secundary: Adenosine Triphosphate/metabolism
Computational Biology
Gene Expression Profiling
Humans
Metabolic Networks and Pathways
Models, Biological
Molecular Chaperones/genetics
Neoplasms/genetics
Neurodegenerative Diseases/genetics
Neurodegenerative Diseases/metabolism
Protein Interaction Maps
Proteome/genetics
Proteome/metabolism
Proteostasis Deficiencies/genetics
Proteostasis Deficiencies/metabolism
Software
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Molecular Chaperones); 0 (Proteome); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Entry month:1801
[Cu] Class update date: 180128
[Lr] Last revision date:180128
[Js] Journal subset:IM
[Da] Date of entry for processing:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005890

  3 / 568 MEDLINE  
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[PMID]: 29317520
[Au] Autor:Lee JH; Mand MR; Kao CH; Zhou Y; Ryu SW; Richards AL; Coon JJ; Paull TT
[Ad] Address:Howard Hughes Medical Institute, Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
[Ti] Title:ATM directs DNA damage responses and proteostasis via genetically separable pathways.
[So] Source:Sci Signal;11(512), 2018 Jan 09.
[Is] ISSN:1937-9145
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The protein kinase ATM is a master regulator of the DNA damage response but also responds directly to oxidative stress. Loss of ATM causes ataxia telangiectasia, a neurodegenerative disorder with pleiotropic symptoms that include cerebellar dysfunction, cancer, diabetes, and premature aging. We genetically separated the activation of ATM by DNA damage from that by oxidative stress using separation-of-function mutations. We found that deficient activation of ATM by the Mre11-Rad50-Nbs1 complex and DNA double-strand breaks resulted in loss of cell viability, checkpoint activation, and DNA end resection in response to DNA damage. In contrast, loss of oxidative activation of ATM had minimal effects on DNA damage-related outcomes but blocked ATM-mediated initiation of checkpoint responses after oxidative stress and resulted in deficiencies in mitochondrial function and autophagy. In addition, expression of a variant ATM incapable of activation by oxidative stress resulted in widespread protein aggregation. These results indicate a direct relationship between the mechanism of ATM activation and its effects on cellular metabolism and DNA damage responses in human cells and implicate ATM in the control of protein homeostasis.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180110
[Lr] Last revision date:180110
[St] Status:In-Data-Review

  4 / 568 MEDLINE  
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[PMID]: 28821618
[Au] Autor:Privat N; Levavasseur E; Yildirim S; Hannaoui S; Brandel JP; Laplanche JL; Béringue V; Seilhean D; Haïk S
[Ad] Address:From the INSERM, UMR S1127, 75013 Paris, France.
[Ti] Title:Region-specific protein misfolding cyclic amplification reproduces brain tropism of prion strains.
[So] Source:J Biol Chem;292(40):16688-16696, 2017 Oct 06.
[Is] ISSN:1083-351X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Human prion diseases such as Creutzfeldt-Jakob disease are transmissible brain proteinopathies, characterized by the accumulation of a misfolded isoform of the host cellular prion protein (PrP) in the brain. According to the prion model, prions are defined as proteinaceous infectious particles composed solely of this abnormal isoform of PrP (PrP ). Even in the absence of genetic material, various prion strains can be propagated in experimental models. They can be distinguished by the pattern of disease they produce and especially by the localization of PrP deposits within the brain and the spongiform lesions they induce. The mechanisms involved in this strain-specific targeting of distinct brain regions still are a fundamental, unresolved question in prion research. To address this question, we exploited a prion conversion assay, protein misfolding cyclic amplification (PMCA), by using experimental scrapie and human prion strains as seeds and specific brain regions from mice and humans as substrates. We show here that region-specific PMCA in part reproduces the specific brain targeting observed in experimental, acquired, and sporadic Creutzfeldt-Jakob diseases. Furthermore, we provide evidence that, in addition to cellular prion protein, other region- and species-specific molecular factors influence the strain-dependent prion conversion process. This important step toward understanding prion strain propagation in the human brain may impact research on the molecular factors involved in protein misfolding and the development of ultrasensitive methods for diagnosing prion disease.
[Mh] MeSH terms primary: Brain/metabolism
Creutzfeldt-Jakob Syndrome/metabolism
PrPSc Proteins/metabolism
Protein Folding
Proteostasis Deficiencies/metabolism
[Mh] MeSH terms secundary: Animals
Brain/pathology
Creutzfeldt-Jakob Syndrome/genetics
Creutzfeldt-Jakob Syndrome/pathology
Humans
Mice
Mice, Transgenic
PrPSc Proteins/genetics
Protein Isoforms/genetics
Protein Isoforms/metabolism
Proteostasis Deficiencies/genetics
Proteostasis Deficiencies/pathology
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (PrPSc Proteins); 0 (Protein Isoforms)
[Em] Entry month:1710
[Cu] Class update date: 171011
[Lr] Last revision date:171011
[Js] Journal subset:IM
[Da] Date of entry for processing:170820
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.793646

  5 / 568 MEDLINE  
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[PMID]: 28765400
[Au] Autor:Mukherjee A; Morales-Scheihing D; Salvadores N; Moreno-Gonzalez I; Gonzalez C; Taylor-Presse K; Mendez N; Shahnawaz M; Gaber AO; Sabek OM; Fraga DW; Soto C
[Ad] Address:Mitchell Center for Alzheimer's Disease, Department of Neurology, John P. and Kathrine G. McGovern Medical School, University of Texas Medical School at Houston, Houston, TX.
[Ti] Title:Induction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanism.
[So] Source:J Exp Med;214(9):2591-2610, 2017 Sep 04.
[Is] ISSN:1540-9538
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Although a large proportion of patients with type 2 diabetes (T2D) accumulate misfolded aggregates composed of the islet amyloid polypeptide (IAPP), its role in the disease is unknown. Here, we show that pancreatic IAPP aggregates can promote the misfolding and aggregation of endogenous IAPP in islet cultures obtained from transgenic mouse or healthy human pancreas. Islet homogenates immunodepleted with anti-IAPP-specific antibodies were not able to induce IAPP aggregation. Importantly, intraperitoneal inoculation of pancreatic homogenates containing IAPP aggregates into transgenic mice expressing human IAPP dramatically accelerates IAPP amyloid deposition, which was accompanied by clinical abnormalities typical of T2D, including hyperglycemia, impaired glucose tolerance, and a substantial reduction on ß cell number and mass. Finally, induction of IAPP deposition and diabetic abnormalities were also induced in vivo by administration of IAPP aggregates prepared in vitro using pure, synthetic IAPP. Our findings suggest that some of the pathologic and clinical alterations of T2D might be transmissible through a similar mechanism by which prions propagate in prion diseases.
[Mh] MeSH terms primary: Diabetes Mellitus, Type 2/metabolism
Islet Amyloid Polypeptide/metabolism
Islets of Langerhans/metabolism
[Mh] MeSH terms secundary: Animals
Diabetes Mellitus, Type 2/etiology
Diabetes Mellitus, Type 2/pathology
Female
Humans
Islets of Langerhans/pathology
Male
Mice
Mice, Transgenic
Prions/metabolism
Protein Aggregates
Proteostasis Deficiencies/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Islet Amyloid Polypeptide); 0 (Prions); 0 (Protein Aggregates)
[Em] Entry month:1709
[Cu] Class update date: 170928
[Lr] Last revision date:170928
[Js] Journal subset:IM
[Da] Date of entry for processing:170803
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20161134

  6 / 568 MEDLINE  
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[PMID]: 28724527
[Au] Autor:Victoria GS; Zurzolo C
[Ad] Address:Unité de Trafic Membranaire et Pathogénèse, Institut Pasteur, Paris, France.
[Ti] Title:The spread of prion-like proteins by lysosomes and tunneling nanotubes: Implications for neurodegenerative diseases.
[So] Source:J Cell Biol;216(9):2633-2644, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Progression of pathology in neurodegenerative diseases is hypothesized to be a non-cell-autonomous process that may be mediated by the productive spreading of prion-like protein aggregates from a "donor cell" that is the source of misfolded aggregates to an "acceptor cell" in which misfolding is propagated by conversion of the normal protein. Although the proteins involved in the various diseases are unrelated, common pathways appear to be used for their intercellular propagation and spreading. Here, we summarize recent evidence of the molecular mechanisms relevant for the intercellular trafficking of protein aggregates involved in prion, Alzheimer's, Huntington's, and Parkinson's diseases. We focus in particular on the common roles that lysosomes and tunneling nanotubes play in the formation and spreading of prion-like assemblies.
[Mh] MeSH terms primary: Lysosomes/metabolism
Nanotubes
Neurodegenerative Diseases/metabolism
Prions/metabolism
Proteostasis Deficiencies/metabolism
[Mh] MeSH terms secundary: Animals
GPI-Linked Proteins/chemistry
GPI-Linked Proteins/metabolism
Humans
Lysosomes/pathology
Nerve Degeneration
Neurodegenerative Diseases/pathology
Prions/chemistry
Protein Aggregates
Protein Aggregation, Pathological
Protein Conformation
Protein Folding
Protein Transport
Proteostasis Deficiencies/pathology
Signal Transduction
Structure-Activity Relationship
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (GPI-Linked Proteins); 0 (PRND protein, human); 0 (Prions); 0 (Protein Aggregates)
[Em] Entry month:1710
[Cu] Class update date: 171004
[Lr] Last revision date:171004
[Js] Journal subset:IM
[Da] Date of entry for processing:170721
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201701047

  7 / 568 MEDLINE  
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[PMID]: 28673927
[Au] Autor:Jayaprakash NG; Surolia A
[Ad] Address:Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
[Ti] Title:Role of glycosylation in nucleating protein folding and stability.
[So] Source:Biochem J;474(14):2333-2347, 2017 Jul 03.
[Is] ISSN:1470-8728
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Glycosylation constitutes one of the most common, ubiquitous and complex forms of post-translational modification. It commences with the synthesis of the protein and plays a significant role in deciding its folded state, oligomerization and thus its function. Recent studies have demonstrated that N-linked glycans help proteins to fold as the stability and folding kinetics are altered with the removal of the glycans from them. Several studies have shown that it alters not only the thermodynamic stability but also the structural features of the folded proteins modulating their interactions and functions. Their inhibition and perturbations have been implicated in diseases from diabetes to degenerative disorders. The intent of this review is to provide insight into the recent advancements in the general understanding on the aspect of glycosylation driven stability of proteins that is imperative to their function and finally their role in health and disease states.
[Mh] MeSH terms primary: Glycoside Hydrolases/metabolism
Glycosyltransferases/metabolism
Models, Biological
Models, Molecular
Protein Processing, Post-Translational
Proteins/metabolism
[Mh] MeSH terms secundary: Animals
Asparagine/metabolism
Glycosylation
Humans
Kinetics
Protein Conformation
Protein Folding
Protein Multimerization
Protein Stability
Proteins/chemistry
Proteostasis Deficiencies/enzymology
Proteostasis Deficiencies/metabolism
Thermodynamics
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Proteins); 7006-34-0 (Asparagine); EC 2.4.- (Glycosyltransferases); EC 3.2.1.- (Glycoside Hydrolases)
[Em] Entry month:1707
[Cu] Class update date: 170726
[Lr] Last revision date:170726
[Js] Journal subset:IM
[Da] Date of entry for processing:170705
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170111

  8 / 568 MEDLINE  
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[PMID]: 28542401
[Au] Autor:Wen J; Scoles DR; Facelli JC
[Ad] Address:Department of Biomedical Informatics, University of Utah, Salt Lake City, Utah, United States of America.
[Ti] Title:Molecular dynamics analysis of the aggregation propensity of polyglutamine segments.
[So] Source:PLoS One;12(5):e0178333, 2017.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Protein misfolding and aggregation is a pathogenic feature shared among at least ten polyglutamine (polyQ) neurodegenerative diseases. While solvent-solution interaction is a key factor driving protein folding and aggregation, the solvation properties of expanded polyQ tracts are not well understood. By using GPU-enabled all-atom molecular dynamics simulations of polyQ monomers in an explicit solvent environment, this study shows that solvent-polyQ interaction propensity decreases as the lengths of polyQ tract increases. This study finds a predominance in long-distance interactions between residues far apart in polyQ sequences with longer polyQ segments, that leads to significant conformational differences. This study also indicates that large loops, comprised of parallel ß-structures, appear in long polyQ tracts and present new aggregation building blocks with aggregation driven by long-distance intra-polyQ interactions. Finally, consistent with previous observations using coarse-grain simulations, this study demonstrates that there is a gain in the aggregation propensity with increased polyQ length, and that this gain is correlated with decreasing ability of solvent-polyQ interaction. These results suggest the modulation of solvent-polyQ interactions as a possible therapeutic strategy for treating polyQ diseases.
[Mh] MeSH terms primary: Peptides/metabolism
[Mh] MeSH terms secundary: Hydrogen Bonding
Molecular Dynamics Simulation
Peptides/chemistry
Protein Aggregation, Pathological/metabolism
Protein Conformation, beta-Strand
Protein Structure, Secondary
Proteostasis Deficiencies/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Peptides); 26700-71-0 (polyglutamine)
[Em] Entry month:1709
[Cu] Class update date: 170919
[Lr] Last revision date:170919
[Js] Journal subset:IM
[Da] Date of entry for processing:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178333

  9 / 568 MEDLINE  
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[PMID]: 28498720
[Au] Autor:Chiti F; Dobson CM
[Ad] Address:Department of Experimental and Clinical Biomedical Sciences "Mario Serio," Section of Biochemistry, Università di Firenze, 50134 Firenze, Italy; email: fabrizio.chiti@unifi.it.
[Ti] Title:Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
[So] Source:Annu Rev Biochem;86:27-68, 2017 Jun 20.
[Is] ISSN:1545-4509
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Peptides and proteins have been found to possess an inherent tendency to convert from their native functional states into intractable amyloid aggregates. This phenomenon is associated with a range of increasingly common human disorders, including Alzheimer and Parkinson diseases, type II diabetes, and a number of systemic amyloidoses. In this review, we describe this field of science with particular reference to the advances that have been made over the last decade in our understanding of its fundamental nature and consequences. We list the proteins that are known to be deposited as amyloid or other types of aggregates in human tissues and the disorders with which they are associated, as well as the proteins that exploit the amyloid motif to play specific functional roles in humans. In addition, we summarize the genetic factors that have provided insight into the mechanisms of disease onset. We describe recent advances in our knowledge of the structures of amyloid fibrils and their oligomeric precursors and of the mechanisms by which they are formed and proliferate to generate cellular dysfunction. We show evidence that a complex proteostasis network actively combats protein aggregation and that such an efficient system can fail in some circumstances and give rise to disease. Finally, we anticipate the development of novel therapeutic strategies with which to prevent or treat these highly debilitating and currently incurable conditions.
[Mh] MeSH terms primary: Alzheimer Disease/history
Amyloid/chemistry
Amyloidosis/history
Diabetes Mellitus, Type 2/history
Parkinson Disease/history
Proteostasis Deficiencies/history
[Mh] MeSH terms secundary: Alzheimer Disease/drug therapy
Alzheimer Disease/metabolism
Alzheimer Disease/pathology
Amyloid/genetics
Amyloid/metabolism
Amyloidosis/drug therapy
Amyloidosis/metabolism
Amyloidosis/pathology
Diabetes Mellitus, Type 2/drug therapy
Diabetes Mellitus, Type 2/metabolism
Diabetes Mellitus, Type 2/pathology
Drugs, Investigational
Gene Expression Regulation
History, 21st Century
Humans
Immunoglobulin Light-chain Amyloidosis
Molecular Chaperones/genetics
Molecular Chaperones/metabolism
Molecular Targeted Therapy
Parkinson Disease/drug therapy
Parkinson Disease/metabolism
Parkinson Disease/pathology
Protein Aggregation, Pathological/history
Protein Aggregation, Pathological/metabolism
Protein Aggregation, Pathological/pathology
Protein Aggregation, Pathological/prevention & control
Protein Conformation
Protein Folding
Proteostasis Deficiencies/drug therapy
Proteostasis Deficiencies/metabolism
Proteostasis Deficiencies/pathology
Proteostasis Deficiencies/prevention & control
[Pt] Publication type:HISTORICAL ARTICLE; JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Amyloid); 0 (Drugs, Investigational); 0 (Molecular Chaperones)
[Em] Entry month:1707
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:170513
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-biochem-061516-045115

  10 / 568 MEDLINE  
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[PMID]: 28489421
[Au] Autor:Sontag EM; Samant RS; Frydman J
[Ad] Address:Department of Biology, Stanford University, Stanford, California 94305; email: emsontag@stanford.edu , rsamant@stanford.edu , jfrydman@stanford.edu.
[Ti] Title:Mechanisms and Functions of Spatial Protein Quality Control.
[So] Source:Annu Rev Biochem;86:97-122, 2017 Jun 20.
[Is] ISSN:1545-4509
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:A healthy proteome is essential for cell survival. Protein misfolding is linked to a rapidly expanding list of human diseases, ranging from neurodegenerative diseases to aging and cancer. Many of these diseases are characterized by the accumulation of misfolded proteins in intra- and extracellular inclusions, such as amyloid plaques. The clear link between protein misfolding and disease highlights the need to better understand the elaborate machinery that manages proteome homeostasis, or proteostasis, in the cell. Proteostasis depends on a network of molecular chaperones and clearance pathways involved in the recognition, refolding, and/or clearance of aberrant proteins. Recent studies reveal that an integral part of the cellular management of misfolded proteins is their spatial sequestration into several defined compartments. Here, we review the properties, function, and formation of these compartments. Spatial sequestration plays a central role in protein quality control and cellular fitness and represents a critical link to the pathogenesis of protein aggregation-linked diseases.
[Mh] MeSH terms primary: Aging/metabolism
Molecular Chaperones/metabolism
Neurodegenerative Diseases/metabolism
Protein Aggregation, Pathological/metabolism
Proteostasis Deficiencies/metabolism
[Mh] MeSH terms secundary: Aging/genetics
Aging/pathology
Amyloidogenic Proteins/chemistry
Amyloidogenic Proteins/genetics
Amyloidogenic Proteins/metabolism
Cell Compartmentation
Gene Expression Regulation
Humans
Molecular Chaperones/genetics
Neurodegenerative Diseases/genetics
Neurodegenerative Diseases/pathology
Prion Proteins/chemistry
Prion Proteins/genetics
Prion Proteins/metabolism
Protein Aggregation, Pathological/genetics
Protein Aggregation, Pathological/pathology
Protein Biosynthesis
Protein Conformation
Protein Folding
Protein Refolding
Proteolysis
Proteostasis Deficiencies/genetics
Proteostasis Deficiencies/pathology
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Amyloidogenic Proteins); 0 (Molecular Chaperones); 0 (Prion Proteins)
[Em] Entry month:1707
[Cu] Class update date: 170704
[Lr] Last revision date:170704
[Js] Journal subset:IM
[Da] Date of entry for processing:170511
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-biochem-060815-014616


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