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Article ; Online: Nucleus-cytoplasm cross-talk in the aging brain.

Benvegnù, Stefano

2019 Volume 98, Issue 2, Page(s) 247–261

Abstract: Aging is a primary risk factor for fatal neurodegenerative disorders, yet the mechanisms underlying physiological healthy aging and pathological aging, and how these mechanisms can divert one scenario to the other, are not completely understood. In ... ...

Abstract	Aging is a primary risk factor for fatal neurodegenerative disorders, yet the mechanisms underlying physiological healthy aging and pathological aging, and how these mechanisms can divert one scenario to the other, are not completely understood. In recent years, reports indicate that alterations in nucleocytoplasmic transport may be a hallmark of both healthy and pathological aging. In this review, I summarize recent evidence supporting this information, specifically focusing on the association between the nucleocytoplasmic transport and aging of the brain, indicating both common and case-specific mechanisms and their interplay, and pointing out alterations of these mechanisms as regulatory "switches" for the fate of the aging brain. Importantly, some of these alterations are intervenable druggable targets, paving the way to a future pharmacotherapeutic intervention.
MeSH term(s)	Aging/metabolism ; Aging/pathology ; Animals ; Brain/metabolism ; Brain/pathology ; Cell Nucleus/metabolism ; Cell Nucleus/pathology ; Cytoplasm/metabolism ; Cytoplasm/pathology ; Humans ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology
Language	English
Publishing date	2019-05-26
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	195324-2
ISSN	1097-4547 ; 0360-4012
ISSN (online)	1097-4547
ISSN	0360-4012
DOI	10.1002/jnr.24446
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Article ; Online: Molecular alterations contributing to brain aging.

Martín-Segura, Adrián / Benvegnù, Stefano

Journal of neuroscience research

2019 Volume 98, Issue 2, Page(s) 231–233

MeSH term(s)	Aging/metabolism ; Animals ; Brain/metabolism ; Epigenesis, Genetic/physiology ; Humans ; Neurons/metabolism ; Protein Transport/physiology
Language	English
Publishing date	2019-09-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	195324-2
ISSN	1097-4547 ; 0360-4012
ISSN (online)	1097-4547
ISSN	0360-4012
DOI	10.1002/jnr.24523
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Article ; Online: Small-molecule inhibitors of carboxylesterase Notum.

Zhao, Yuguang / Jolly, Sarah / Benvegnu, Stefano / Jones, E Yvonne / Fish, Paul V

Future medicinal chemistry

2021 Volume 13, Issue 11, Page(s) 1001–1015

Abstract: Notum has recently been identified as a negative regulator of Wnt signaling through the removal of an essential palmitoleate group from Wnt proteins. There are emerging reports that Notum plays a role in human disease, with published data suggesting that ...

Abstract	Notum has recently been identified as a negative regulator of Wnt signaling through the removal of an essential palmitoleate group from Wnt proteins. There are emerging reports that Notum plays a role in human disease, with published data suggesting that targeting Notum could represent a new therapeutic approach for treating cancer, osteoporosis and neurodegenerative disorders. Complementary hit-finding strategies have been applied with successful approaches that include high-throughput screening, activity-based protein profiling, screening of fragment libraries and virtual screening campaigns. Structural studies are accelerating the discovery of new inhibitors of Notum. Three fit-for-purpose examples are LP-922056, ABC99 and ARUK3001185. The application of these small-molecule inhibitors is helping to further advance an understanding of the role Notum plays in human disease.
MeSH term(s)	Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Esterases/antagonists & inhibitors ; Esterases/metabolism ; Humans ; Models, Molecular ; Molecular Structure ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology
Chemical Substances	Enzyme Inhibitors ; Small Molecule Libraries ; Esterases (EC 3.1.-) ; Notum protein, human (EC 3.1.1.-)
Language	English
Publishing date	2021-04-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1756-8927
ISSN (online)	1756-8927
DOI	10.4155/fmc-2021-0036
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Article ; Online: E3 ligase mahogunin (MGRN1) influences amyloid precursor protein maturation and secretion.

Benvegnù, Stefano / Wahle, Tina / Dotti, Carlos G

Oncotarget

2017 Volume 8, Issue 52, Page(s) 89439–89450

Abstract: Altered processing of the Amyloid Precursor Protein (APP) is a well-recognized central pathogenic mechanism in Alzheimer's Disease (AD), and regulation of APP processing is a major focus of research in the AD field. However, how age-associated cellular ... ...

Abstract	Altered processing of the Amyloid Precursor Protein (APP) is a well-recognized central pathogenic mechanism in Alzheimer's Disease (AD), and regulation of APP processing is a major focus of research in the AD field. However, how age-associated cellular and molecular changes contribute to changes in the amyloidogenic processing of APP have not been extensively clarified so far. We here provide evidence that the processing of APP is influenced by the e3 ubiquitin ligase Mahogunin (MGRN1), a neuroprotective molecule whose levels decrease with aging. Specifically, the expression of MGRN1 inhibits the maturation of APP by sequestering it in the secretory pathway. This sequestration significantly delayed the proteolytic processing of APP, resulting in a reduced β-amyloid (Aβ) peptide release into the extracellular environment. Accordingly, a reduction of MGRN1 levels in hippocampal neurons, as it occurs during physiological aging, leads to an increased Aβ40 and Aβ42 release. We therefore propose that age contributes to the amyloidogenic processing of APP by altering its intracellular trafficking along the secretory pathway due in part to the down-regulation of MGRN1.
Language	English
Publishing date	2017-10-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.20143
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Article ; Online: Epigenetic repression of Wnt receptors in AD: a role for Sirtuin2-induced H4K16ac deacetylation of Frizzled1 and Frizzled7 promoters.

Palomer, Ernest / Martín-Flores, Núria / Jolly, Sarah / Pascual-Vargas, Patricia / Benvegnù, Stefano / Podpolny, Marina / Teo, Samuel / Vaher, Kadi / Saito, Takashi / Saido, Takaomi C / Whiting, Paul / Salinas, Patricia C

Molecular psychiatry

2022 Volume 27, Issue 7, Page(s) 3024–3033

Abstract: Growing evidence supports a role for deficient Wnt signalling in Alzheimer's disease (AD). First, the Wnt antagonist DKK1 is elevated in AD brains and is required for amyloid-β-induced synapse loss. Second, LRP6 Wnt co-receptor is required for synapse ... ...

Abstract	Growing evidence supports a role for deficient Wnt signalling in Alzheimer's disease (AD). First, the Wnt antagonist DKK1 is elevated in AD brains and is required for amyloid-β-induced synapse loss. Second, LRP6 Wnt co-receptor is required for synapse integrity and three variants of this receptor are linked to late-onset AD. However, the expression/role of other Wnt signalling components remain poorly explored in AD. Wnt receptors Frizzled1 (Fzd1), Fzd5, Fzd7 and Fzd9 are of interest due to their role in synapse formation/plasticity. Our analyses showed reduced FZD1 and FZD7 mRNA levels in the hippocampus of human early AD stages and in the hAPP
MeSH term(s)	Alzheimer Disease/genetics ; Animals ; Epigenetic Repression ; Frizzled Receptors ; Humans ; Mice ; RNA, Messenger ; Receptors, Wnt ; Sirtuin 1 ; Sirtuin 2 ; Wnt Signaling Pathway
Chemical Substances	FZD1 protein, human ; FZD7 protein, human ; Frizzled Receptors ; Fzd1 protein, mouse ; Fzd7 protein, mouse ; RNA, Messenger ; Receptors, Wnt ; SIRT1 protein, human (EC 3.5.1.-) ; Sirt2 protein, mouse (EC 3.5.1.-) ; Sirtuin 1 (EC 3.5.1.-) ; Sirtuin 2 (EC 3.5.1.-)
Language	English
Publishing date	2022-03-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1330655-8
ISSN	1476-5578 ; 1359-4184
ISSN (online)	1476-5578
ISSN	1359-4184
DOI	10.1038/s41380-022-01492-z
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Article: Aging Triggers Cytoplasmic Depletion and Nuclear Translocation of the E3 Ligase Mahogunin: A Function for Ubiquitin in Neuronal Survival

Benvegnù, Stefano / Carlos G. Dotti / Ernest Palomer / Jerónimo Jurado-Arjona / María Inés Mateo

Molecular cell. 2017 May 04, v. 66, no. 3

2017

Abstract: A decline in proteasome function is causally connected to neuronal aging and aging-associated neuropathologies. By using hippocampal neurons in culture and in vivo, we show that aging triggers a reduction and a cytoplasm-to-nucleus redistribution of the ... ...

Abstract	A decline in proteasome function is causally connected to neuronal aging and aging-associated neuropathologies. By using hippocampal neurons in culture and in vivo, we show that aging triggers a reduction and a cytoplasm-to-nucleus redistribution of the E3 ubiquitin ligase mahogunin (MGRN1). Proteasome impairment induces MGRN1 monoubiquitination, the key post-translational modification for its nuclear entry. One potential mechanism for MGRN1 monoubiquitination is via progressive deubiquitination at the proteasome of polyubiquitinated MGRN1. Once in the nucleus, MGRN1 potentiates the transcriptional cellular response to proteotoxic stress. Inhibition of MGRN1 impairs ATF3-mediated neuronal responsiveness to proteosomal stress and increases neuronal stress, while increasing MGRN1 ameliorates signs of neuronal aging, including cognitive performance in old animals. Our results imply that, among others, the strength of neuronal survival in a proteasomal deterioration background, like during aging, depends on the fine-tuning of ubiquitination-deubiquitination.
Keywords	cognition ; elderly ; neurons ; post-translational modification ; proteasome endopeptidase complex ; transcription (genetics) ; ubiquitin ; ubiquitin-protein ligase
Language	English
Dates of publication	2017-0504
Size	p. 358-372.e7.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2017.04.005
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Article ; Online: Aging Triggers Cytoplasmic Depletion and Nuclear Translocation of the E3 Ligase Mahogunin: A Function for Ubiquitin in Neuronal Survival.

Benvegnù, Stefano / Mateo, María Inés / Palomer, Ernest / Jurado-Arjona, Jerónimo / Dotti, Carlos G

Molecular cell

2017 Volume 66, Issue 3, Page(s) 358–372.e7

Abstract	A decline in proteasome function is causally connected to neuronal aging and aging-associated neuropathologies. By using hippocampal neurons in culture and in vivo, we show that aging triggers a reduction and a cytoplasm-to-nucleus redistribution of the E3 ubiquitin ligase mahogunin (MGRN1). Proteasome impairment induces MGRN1 monoubiquitination, the key post-translational modification for its nuclear entry. One potential mechanism for MGRN1 monoubiquitination is via progressive deubiquitination at the proteasome of polyubiquitinated MGRN1. Once in the nucleus, MGRN1 potentiates the transcriptional cellular response to proteotoxic stress. Inhibition of MGRN1 impairs ATF3-mediated neuronal responsiveness to proteosomal stress and increases neuronal stress, while increasing MGRN1 ameliorates signs of neuronal aging, including cognitive performance in old animals. Our results imply that, among others, the strength of neuronal survival in a proteasomal deterioration background, like during aging, depends on the fine-tuning of ubiquitination-deubiquitination.
MeSH term(s)	Activating Transcription Factor 3/genetics ; Activating Transcription Factor 3/metabolism ; Active Transport, Cell Nucleus ; Aging/genetics ; Aging/metabolism ; Aging/pathology ; Animals ; Behavior, Animal ; Cell Nucleus/enzymology ; Cell Nucleus/ultrastructure ; Cell Survival ; Chromatin/enzymology ; Cognition ; Cytoplasm/enzymology ; HEK293 Cells ; Hippocampus/enzymology ; Hippocampus/ultrastructure ; Humans ; Maze Learning ; Mice, Inbred C57BL ; Neurons/enzymology ; Neurons/ultrastructure ; Proteasome Endopeptidase Complex/metabolism ; RNA Interference ; Rats, Wistar ; Signal Transduction ; Stress, Physiological ; Transcription, Genetic ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Activating Transcription Factor 3 ; Chromatin ; Ubiquitin ; MGRN1 protein, human (EC 2.3.2.27) ; Mgrn1 protein, mouse (EC 2.3.2.27) ; Mgrn1 protein, rat (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2017-05-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2017.04.005
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Article ; Online: Neuronal activity controls Bdnf expression via Polycomb de-repression and CREB/CBP/JMJD3 activation in mature neurons.

Palomer, Ernest / Carretero, Javier / Benvegnù, Stefano / Dotti, Carlos G / Martin, Mauricio G

Nature communications

2016 Volume 7, Page(s) 11081

Abstract: It has been recently described that in embryonic stem cells, the expression of some important developmentally regulated genes is repressed, but poised for fast activation under the appropriate stimuli. In this work we show that Bdnf promoters are ... ...

Abstract	It has been recently described that in embryonic stem cells, the expression of some important developmentally regulated genes is repressed, but poised for fast activation under the appropriate stimuli. In this work we show that Bdnf promoters are repressed by Polycomb Complex 2 in mature hippocampal neurons, and basal expression is guaranteed by the coexistence with activating histone marks. Neuronal stimulation triggered by N-methyl-D-aspartate application induces the transcription of these promoters by H3K27Me3 demethylation and H3K27Me3 phosphorylation at Serine 28 leading to displacement of EZH2, the catalytic subunit of Polycomb Repressor Complex 2. Our data show that the fast transient expression of Bdnf promoters II and VI after neuronal stimulation is dependent on acetylation of histone H3K27 by CREB-p/CBP. Thus, regulatory mechanisms established during development seem to remain after differentiation controlling genes induced by different stimuli, as would be the case of early memory genes in mature neurons.
MeSH term(s)	Acetylation/drug effects ; Animals ; Brain-Derived Neurotrophic Factor/genetics ; Brain-Derived Neurotrophic Factor/metabolism ; CREB-Binding Protein/metabolism ; Cell Differentiation ; Cyclic AMP Response Element-Binding Protein/metabolism ; Enhancer of Zeste Homolog 2 Protein ; Epigenesis, Genetic/drug effects ; Gene Expression Regulation, Developmental/drug effects ; Hippocampus/cytology ; Histones/metabolism ; Jumonji Domain-Containing Histone Demethylases/metabolism ; Long-Term Synaptic Depression/drug effects ; Lysine/metabolism ; Methylation/drug effects ; Models, Biological ; N-Methylaspartate/pharmacology ; Neurons/cytology ; Neurons/metabolism ; Phosphorylation/drug effects ; Polycomb Repressive Complex 2/metabolism ; Polycomb-Group Proteins/metabolism ; Promoter Regions, Genetic/genetics ; Rats, Wistar
Chemical Substances	Brain-Derived Neurotrophic Factor ; Cyclic AMP Response Element-Binding Protein ; Histones ; Polycomb-Group Proteins ; N-Methylaspartate (6384-92-5) ; Jumonji Domain-Containing Histone Demethylases (EC 1.14.11.-) ; Kdm6b protein, rat (EC 1.14.11.-) ; EZH2 protein, rat (EC 2.1.1.43) ; Enhancer of Zeste Homolog 2 Protein (EC 2.1.1.43) ; Polycomb Repressive Complex 2 (EC 2.1.1.43) ; CREB-Binding Protein (EC 2.3.1.48) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2016-03-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/ncomms11081
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Article ; Online: Aged PrP null mice show defective processing of neuregulins in the peripheral nervous system.

Benvegnù, Stefano / Gasperini, Lisa / Legname, Giuseppe

Molecular and cellular neurosciences

2011 Volume 47, Issue 1, Page(s) 28–35

Abstract: A prion, a protease-resistant conformer of the cellular prion protein (PrP(C)), is the causative agent of transmissible spongiform encephalopathies or prion diseases. While this property is well established for the aberrantly folded protein, the ... ...

Abstract	A prion, a protease-resistant conformer of the cellular prion protein (PrP(C)), is the causative agent of transmissible spongiform encephalopathies or prion diseases. While this property is well established for the aberrantly folded protein, the physiological function of PrP(C) remains elusive. Among different putative functions, the non-pathogenic protein isoform PrP(C) is involved in several cellular processes. Here, we show that PrP(C) regulates the cleavage of neuregulin-1 proteins (NRG1). Neuregulins provide key axonal signals that regulate several processes, including glial cells proliferation, survival and myelination. Interestingly, mice devoid of PrP(C) (Prnp⁰/⁰) were recently shown to have a late-onset demyelinating disease in the peripheral nervous system (PNS) but not in the central nervous system (CNS). We found that NRG1 processing is developmentally regulated in the PNS and, by comparing wildtype and Prnp⁰/⁰ mice, that PrP(C) influences NRG1 processing in old, but not in young, animals. In addition, we found that also the processing of neuregulin-3, another neuregulin family member, is altered in the PNS of Prnp⁰/⁰ mice. These differences in neuregulin proteins processing are not paralleled in the CNS, thus suggesting a different cellular function for PrP(C) between the CNS and the PNS.
MeSH term(s)	Aging/physiology ; Animals ; Cells, Cultured ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neuregulins/metabolism ; Peripheral Nervous System/physiopathology ; Prions/genetics ; Prions/metabolism ; Proto-Oncogene Proteins c-fyn/metabolism ; Sciatic Nerve/cytology ; Sciatic Nerve/metabolism ; Signal Transduction/physiology
Chemical Substances	Neuregulins ; Prions ; Proto-Oncogene Proteins c-fyn (EC 2.7.10.2) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2011-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1046640-x
ISSN	1095-9327 ; 1044-7431
ISSN (online)	1095-9327
ISSN	1044-7431
DOI	10.1016/j.mcn.2011.02.005
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Article ; Online: Design of a Potent, Selective, and Brain-Penetrant Inhibitor of Wnt-Deactivating Enzyme Notum by Optimization of a Crystallographic Fragment Hit.

Willis, Nicky J / Mahy, William / Sipthorp, James / Zhao, Yuguang / Woodward, Hannah L / Atkinson, Benjamin N / Bayle, Elliott D / Svensson, Fredrik / Frew, Sarah / Jeganathan, Fiona / Monaghan, Amy / Benvegnù, Stefano / Jolly, Sarah / Vecchia, Luca / Ruza, Reinis R / Kjær, Svend / Howell, Steven / Snijders, Ambrosius P / Bictash, Magda /

Salinas, Patricia C / Vincent, Jean-Paul / Jones, E Yvonne / Whiting, Paul / Fish, Paul V

Journal of medicinal chemistry

2022 Volume 65, Issue 10, Page(s) 7212–7230

Abstract: Notum is a carboxylesterase that suppresses Wnt signaling through deacylation of an essential palmitoleate group on Wnt proteins. There is a growing understanding of the role Notum plays in human diseases such as colorectal cancer and Alzheimer's disease, ...

Abstract	Notum is a carboxylesterase that suppresses Wnt signaling through deacylation of an essential palmitoleate group on Wnt proteins. There is a growing understanding of the role Notum plays in human diseases such as colorectal cancer and Alzheimer's disease, supporting the need to discover improved inhibitors, especially for use in models of neurodegeneration. Here, we have described the discovery and profile of
MeSH term(s)	Brain/metabolism ; Crystallography, X-Ray ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Esterases/metabolism ; Wnt Signaling Pathway
Chemical Substances	Enzyme Inhibitors ; Esterases (EC 3.1.-)
Language	English
Publishing date	2022-05-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.2c00162
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