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Article: Regulation of the proteostasis network by the neuronal system.

Zhu, Huadong / Cohen, Ehud

2023 Volume 10, Page(s) 1290118

Abstract: The protein homeostasis (proteostasis) network is a nexus of molecular mechanisms that act in concert to maintain the integrity of the proteome and ensure proper cellular and organismal functionality. Early in life the proteostasis network efficiently ... ...

Abstract	The protein homeostasis (proteostasis) network is a nexus of molecular mechanisms that act in concert to maintain the integrity of the proteome and ensure proper cellular and organismal functionality. Early in life the proteostasis network efficiently preserves the functionality of the proteome, however, as the organism ages, or due to mutations or environmental insults, subsets of inherently unstable proteins misfold and form insoluble aggregates that accrue within the cell. These aberrant protein aggregates jeopardize cellular viability and, in some cases, underlie the development of devastating illnesses. Hence, the accumulation of protein aggregates activates different nodes of the proteostasis network that refold aberrantly folded polypeptides, or direct them for degradation. The proteostasis network apparently functions within the cell, however, a myriad of studies indicate that this nexus of mechanisms is regulated at the organismal level by signaling pathways. It was also discovered that the proteostasis network differentially responds to dissimilar proteotoxic insults by tailoring its response according to the specific challenge that cells encounter. In this mini-review, we delineate the proteostasis-regulating neuronal mechanisms, describe the indications that the proteostasis network differentially responds to distinct proteotoxic challenges, and highlight possible future clinical prospects of these insights.
Language	English
Publishing date	2023-11-02
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2023.1290118
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Organismal Protein Homeostasis Mechanisms.

Hoppe, Thorsten / Cohen, Ehud

Genetics

2021 Volume 215, Issue 4, Page(s) 889–901

Abstract: Sustaining a healthy proteome is a lifelong challenge for each individual cell of an organism. However, protein homeostasis or proteostasis is constantly jeopardized since damaged proteins accumulate under proteotoxic stress that originates from ever- ... ...

Abstract	Sustaining a healthy proteome is a lifelong challenge for each individual cell of an organism. However, protein homeostasis or proteostasis is constantly jeopardized since damaged proteins accumulate under proteotoxic stress that originates from ever-changing metabolic, environmental, and pathological conditions. Proteostasis is achieved via a conserved network of quality control pathways that orchestrate the biogenesis of correctly folded proteins, prevent proteins from misfolding, and remove potentially harmful proteins by selective degradation. Nevertheless, the proteostasis network has a limited capacity and its collapse deteriorates cellular functionality and organismal viability, causing metabolic, oncological, or neurodegenerative disorders. While cell-autonomous quality control mechanisms have been described intensely, recent work on
MeSH term(s)	Animals ; Caenorhabditis elegans/physiology ; HSP70 Heat-Shock Proteins/metabolism ; Homeostasis ; Humans ; Protein Folding ; Proteome/metabolism ; Proteostasis ; Proteostasis Deficiencies/physiopathology ; Signal Transduction ; Stress, Physiological
Chemical Substances	HSP70 Heat-Shock Proteins ; Proteome
Language	English
Publishing date	2021-07-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1534/genetics.120.301283
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Article ; Online: Lipid Assemblies at the Crossroads of Aging, Proteostasis, and Neurodegeneration.

Roitenberg, Noa / Cohen, Ehud

Trends in cell biology

2019 Volume 29, Issue 12, Page(s) 954–963

Abstract: The proteostasis network (PN) is a nexus of mechanisms that act in concert to maintain the integrity of the proteome. Efficiency of the PN declines with age, resulting in the accumulation of misfolded proteins, and in some cases in the development of ... ...

Abstract	The proteostasis network (PN) is a nexus of mechanisms that act in concert to maintain the integrity of the proteome. Efficiency of the PN declines with age, resulting in the accumulation of misfolded proteins, and in some cases in the development of neurodegenerative disorders. Thus, maintaining an active and efficient PN through the late stages of life could delay or prevent neurodegeneration. Indeed, altering the activity of aging-regulating pathways protects model organisms from neurodegeneration-linked toxic protein aggregation. Here, we delineate evidence that the formation and integrity of lipid assemblies are affected by aging-regulating pathways, and describe the roles of these structures in proteostasis maintenance. We also highlight future research directions and discuss the possibility that compounds which modulate lipid assemblies could be used for the treatment of neurodegenerative disorders.
MeSH term(s)	Aging/physiology ; Animals ; Humans ; Lipids ; Neurodegenerative Diseases/pathology ; Protein Folding ; Proteome/metabolism ; Proteostasis/physiology ; Proteostasis Deficiencies/pathology
Chemical Substances	Lipids ; Proteome
Language	English
Publishing date	2019-10-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2019.09.003
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Article ; Online: Temporal requirements of SKN-1/NRF as a regulator of lifespan and proteostasis in Caenorhabditis elegans.

Grushko, Danielle / Boocholez, Hana / Levine, Amir / Cohen, Ehud

PloS one

2021 Volume 16, Issue 7, Page(s) e0243522

Abstract: Lowering the activity of the Insulin/IGF-1 Signaling (IIS) cascade results in elevated stress resistance, enhanced protein homeostasis (proteostasis) and extended lifespan of worms, flies and mice. In the nematode Caenorhabditis elegans (C. elegans), the ...

Abstract	Lowering the activity of the Insulin/IGF-1 Signaling (IIS) cascade results in elevated stress resistance, enhanced protein homeostasis (proteostasis) and extended lifespan of worms, flies and mice. In the nematode Caenorhabditis elegans (C. elegans), the longevity phenotype that stems from IIS reduction is entirely dependent upon the activities of a subset of transcription factors including the Forkhead factor DAF-16/FOXO (DAF-16), Heat Shock Factor-1 (HSF-1), SKiNhead/Nrf (SKN-1) and ParaQuat Methylviologen responsive (PQM-1). While DAF-16 determines lifespan exclusively during early adulthood and governs proteostasis in early adulthood and midlife, HSF-1 executes these functions foremost during development. Despite the central roles of SKN-1 as a regulator of lifespan and proteostasis, the temporal requirements of this transcription factor were unknown. Here we employed conditional knockdown techniques and discovered that in C. elegans, SKN-1 is primarily important for longevity and proteostasis during late larval development through early adulthood. Our findings indicate that events that occur during late larval developmental through early adulthood affect lifespan and proteostasis and suggest that subsequent to HSF-1, SKN-1 sets the conditions, partially overlapping temporally with DAF-16, that enable IIS reduction to promote longevity and proteostasis. Our findings raise the intriguing possibility that HSF-1, SKN-1 and DAF-16 function in a coordinated and sequential manner to promote healthy aging.
MeSH term(s)	Animals ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/antagonists & inhibitors ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; DNA-Binding Proteins/antagonists & inhibitors ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Forkhead Transcription Factors/metabolism ; Larva/drug effects ; Larva/growth & development ; Larva/metabolism ; Longevity ; Peptides/pharmacology ; Proteostasis/physiology ; RNA Interference ; RNA, Double-Stranded/metabolism ; Ribonuclease III/antagonists & inhibitors ; Ribonuclease III/genetics ; Ribonuclease III/metabolism ; Transcription Factors/antagonists & inhibitors ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; DNA-Binding Proteins ; Forkhead Transcription Factors ; Peptides ; RNA, Double-Stranded ; Transcription Factors ; daf-16 protein, C elegans ; heat shock factor-1, C elegans ; skn-1 protein, C elegans (148733-36-2) ; polyglutamine (26700-71-0) ; dcr-1 protein, C elegans (EC 3.1.26.-) ; Ribonuclease III (EC 3.1.26.3)
Language	English
Publishing date	2021-07-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0243522
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Article: Aging, protein aggregation, chaperones, and neurodegenerative disorders: mechanisms of coupling and therapeutic opportunities.

Cohen, Ehud

Rambam Maimonides medical journal

2012 Volume 3, Issue 4, Page(s) e0021

Abstract: Late onset is a key unifying feature of human neurodegenerative maladies such as Alzheimer's and Parkinson's diseases and prion disorders. While sporadic cases typically emerge during the patient's seventh decade of life or later, mutation-linked, ... ...

Abstract	Late onset is a key unifying feature of human neurodegenerative maladies such as Alzheimer's and Parkinson's diseases and prion disorders. While sporadic cases typically emerge during the patient's seventh decade of life or later, mutation-linked, familial cases manifest during the fifth or sixth decade. This common temporal emergence pattern raises the prospect that slowing aging may prevent the accumulation of toxic protein aggregates that lead to the development of these disorders, postpone the onset of these maladies, and alleviate their symptoms once emerged. Invertebrate-based studies indicated that reducing the activity of insulin/IGF signaling (IIS), a prominent aging regulatory pathway, protects from neurodegeneration-linked toxic protein aggregation. The validity of this approach has been tested and confirmed in mammals as reducing the activity of the IGF-1 signaling pathway-protected Alzheimer's model mice from the behavioral and biochemical impairments associated with the disease. Here I review the recent advances in the field, describe the known mechanistic links between toxic protein aggregation and the aging process, and delineate the future therapeutic potential of IIS reduction as a treatment for various neurodegenerative disorders.
Language	English
Publishing date	2012-10-31
Publishing country	Israel
Document type	Journal Article
ZDB-ID	2573657-7
ISSN	2076-9172
ISSN	2076-9172
DOI	10.5041/RMMJ.10088
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Article ; Online: Countering neurodegeneration by reducing the activity of the insulin/IGF signaling pathway: current knowledge and future prospects.

Cohen, Ehud

Experimental gerontology

2011 Volume 46, Issue 2-3, Page(s) 124–128

Abstract: Human neurodegenerative maladies share two common key features: a mechanistic link to the accumulation and deposition of aberrantly aggregated proteins and late onset. These similarities among otherwise unrelated disorders suggest that the aging process ... ...

Abstract	Human neurodegenerative maladies share two common key features: a mechanistic link to the accumulation and deposition of aberrantly aggregated proteins and late onset. These similarities among otherwise unrelated disorders suggest that the aging process plays an active role in enabling the emergence of these diseases late in life. Invertebrate-based studies have shown that the manipulation of aging by the reduction of the Insulin/IGF signaling (IIS), a prominent aging regulatory pathway, protects model organisms from neurodegeneration-linked toxic protein aggregation. Recent studies have also indicated that the counter proteotoxic effect of IIS reduction is conserved from worms to mice as reduced IGF-1 signaling protected Alzheimer's-model mice from the disease-like behavioral impairments, pathological phenotypes and premature death typical to these model animals. In this article I review the current knowledge on the protective mechanisms that are suppressed by the IIS and discuss the future therapeutic potential of IIS reduction as a treatment for neurodegenerative disorders.
MeSH term(s)	Aging/metabolism ; Amyloid beta-Peptides/metabolism ; Animals ; Humans ; Insulin/metabolism ; Invertebrates/metabolism ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/therapy ; Signal Transduction ; Somatomedins/antagonists & inhibitors ; Somatomedins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Insulin ; Somatomedins
Language	English
Publishing date	2011-02
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	390992-x
ISSN	1873-6815 ; 0531-5565
ISSN (online)	1873-6815
ISSN	0531-5565
DOI	10.1016/j.exger.2010.08.032
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Article: The Emerging Roles of Early Protein Folding Events in the Secretory Pathway in the Development of Neurodegenerative Maladies.

Dubnikov, Tatyana / Cohen, Ehud

Frontiers in neuroscience

2017 Volume 11, Page(s) 48

Abstract: Although, protein aggregation and deposition are unifying features of various neurodegenerative disorders, recent studies indicate that different mechanisms can lead to the development of the same malady. Among these, failure in early protein folding and ...

Abstract	Although, protein aggregation and deposition are unifying features of various neurodegenerative disorders, recent studies indicate that different mechanisms can lead to the development of the same malady. Among these, failure in early protein folding and maturation emerge as key mechanistic events that lead to the manifestation of a myriad of illnesses including Alzheimer's disease and prion disorders. Here we delineate the cascade of maturation steps that nascent polypeptides undergo in the secretory pathway to become functional proteins, and the chaperones that supervise and assist this process, focusing on the subgroup of proline
Language	English
Publishing date	2017-02-07
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2411902-7
ISSN	1662-453X ; 1662-4548
ISSN (online)	1662-453X
ISSN	1662-4548
DOI	10.3389/fnins.2017.00048
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Article ; Online: Gene expression modulation by the linker of nucleoskeleton and cytoskeleton complex contributes to proteostasis.

Levine, Amir / Grushko, Danielle / Cohen, Ehud

Aging cell

2019 Volume 18, Issue 6, Page(s) e13047

Abstract: Cellular mechanisms that act in concert to maintain protein homeostasis (proteostasis) are vital for organismal functionality and survival. Nevertheless, subsets of aggregation-prone proteins form toxic aggregates (proteotoxicity) that in some cases, ... ...

Abstract	Cellular mechanisms that act in concert to maintain protein homeostasis (proteostasis) are vital for organismal functionality and survival. Nevertheless, subsets of aggregation-prone proteins form toxic aggregates (proteotoxicity) that in some cases, underlie the development of neurodegenerative diseases. Proteotoxic aggregates are often deposited in the vicinity of the nucleus, a process that is cytoskeleton-dependent. Accordingly, cytoskeletal dysfunction contributes to pathological hallmarks of various neurodegenerative diseases. Here, we asked whether the linker of nucleoskeleton and cytoskeleton (LINC) complex, which bridges these filaments across the nuclear envelope, is needed for the maintenance of proteostasis. Employing model nematodes, we discovered that knocking down LINC components impairs the ability of the worm to cope with proteotoxicity. Knocking down anc-1, which encodes a key component of the LINC complex, modulates the expression of transcription factors and E3 ubiquitin ligases, thereby affecting the rates of protein ubiquitination and impairing proteasome-mediated protein degradation. Our results establish a link between the LINC complex, protein degradation, and neurodegeneration-associated proteotoxicity.
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Cytoskeleton/genetics ; Cytoskeleton/metabolism ; Gene Expression Profiling ; Gene Expression Regulation ; Nuclear Matrix/genetics ; Nuclear Matrix/metabolism ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Proteostasis/genetics ; Sequence Analysis, RNA
Chemical Substances	Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2019-10-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113083-8
ISSN	1474-9726 ; 1474-9718
ISSN (online)	1474-9726
ISSN	1474-9718
DOI	10.1111/acel.13047
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Article: Dolomite-based quarry-dust as a substitute for fly-ash geopolymers and cement pastes

Cohen, Ehud / Bar-Nes, Gabriela / Peled, Alva

Journal of cleaner production. 2019 Oct. 20, v. 235

2019

Abstract: The effects of the addition of dolomite-based quarry-dust (QD) waste material as a filler in CEM-I and FA-based geopolymeric mixtures were studied. This study shows that unused QD may be integrated at high replacement rates (up to 40% by weight) in both ... ...

Abstract	The effects of the addition of dolomite-based quarry-dust (QD) waste material as a filler in CEM-I and FA-based geopolymeric mixtures were studied. This study shows that unused QD may be integrated at high replacement rates (up to 40% by weight) in both CEM-I and FA-based systems, showing good and, in some cases, even significant improvement in their engineering properties. A significant increase in compressive strength was found for both CEM- and FA-based mixtures when gradually increasing the QD content. Two main mechanisms were suggested that may support this positive effect: the mechanical anchoring of the QD particles within the matrix, which was mainly found in the FA-based mixtures, due to the significant differences in their particle shape and morphology, and the enhancement of the hydration reaction in the presence of the QD particles mainly found in the CEM-based mixtures. Nevertheless, the vulnerability of these QD containing products to acidic conditions must be carefully considered. The ability to use quarry waste products as construction materials would not only reduce the costs and energy required for production processes but would also provide an efficient, green disposal path for quarry-dust waste, which currently poses an environmental problem without an alternative solution.
Keywords	cement ; compression strength ; construction materials ; energy ; engineering ; fly ash ; pastes ; polymers ; quarries ; wastes
Language	English
Dates of publication	2019-1020
Size	p. 910-919.
Publishing place	Elsevier Ltd
Document type	Article
ISSN	0959-6526
DOI	10.1016/j.jclepro.2019.06.261
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: From mutated genes to familial Alzheimer's disease.

Ben-Gedalya, Tziona / Cohen, Ehud

Cell cycle (Georgetown, Tex.)

2016 Volume 15, Issue 7, Page(s) 877–878

MeSH term(s)	Alzheimer Disease/genetics ; Humans ; Mutation
Language	English
Publishing date	2016-03-03
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.1080/15384101.2016.1151727
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