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Article ; Online: M

Dwomoh, Louis / Rossi, Mario / Scarpa, Miriam / Khajehali, Elham / Molloy, Colin / Herzyk, Pawel / Mistry, Shailesh N / Bottrill, Andrew R / Sexton, Patrick M / Christopoulos, Arthur / Conn, Jeffrey / Lindsley, Craig W / Bradley, Sophie J / Tobin, Andrew B

Science signaling

2022 Volume 15, Issue 760, Page(s) eabm3720

Abstract: Many dementias are propagated through the spread of "prion-like" misfolded proteins. This includes prion diseases themselves (such as Creutzfeldt-Jakob disease) and Alzheimer's disease (AD), for which no treatments are available to slow or stop ... ...

Abstract	Many dementias are propagated through the spread of "prion-like" misfolded proteins. This includes prion diseases themselves (such as Creutzfeldt-Jakob disease) and Alzheimer's disease (AD), for which no treatments are available to slow or stop progression. The M
MeSH term(s)	Humans ; Animals ; Mice ; Prions/genetics ; Neurodegenerative Diseases/genetics ; Pathology, Molecular ; Proteomics ; Prion Diseases/genetics ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Receptor, Muscarinic M1/genetics ; Receptor, Muscarinic M1/metabolism
Chemical Substances	Prions ; Receptor, Muscarinic M1
Language	English
Publishing date	2022-11-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.abm3720
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Article ; Online: Targeting the kinase insert loop of PERK selectively modulates PERK signaling without systemic toxicity in mice.

Hughes, Daniel T / Halliday, Mark / Smith, Heather L / Verity, Nicholas C / Molloy, Colin / Radford, Helois / Butcher, Adrian J / Mallucci, Giovanna R

Science signaling

2020 Volume 13, Issue 644

Abstract: Chronic activation of the unfolded protein response (UPR), notably the branch comprising the kinase PERK and the translation initiation factor eIF2α, is a pathological feature of many neurodegenerative diseases caused by protein misfolding. Partial ... ...

Abstract	Chronic activation of the unfolded protein response (UPR), notably the branch comprising the kinase PERK and the translation initiation factor eIF2α, is a pathological feature of many neurodegenerative diseases caused by protein misfolding. Partial reduction of UPR signaling at the level of phosphorylated eIF2α is neuroprotective and avoids the pancreatic toxicity caused by full inhibition of PERK kinase activity. However, other stress pathways besides the UPR converge on phosphorylated eIF2α in the integrated stress response (ISR), which is critical to normal cellular function. We explored whether partial inhibition of PERK signaling may be a better therapeutic option. PERK-mediated phosphorylation of eIF2α requires its binding to the insert loop within PERK's kinase domain, which is, itself, phosphorylated at multiple sites. We found that, as expected, Akt mediates the phosphorylation of Thr
MeSH term(s)	Acetates/pharmacology ; Animals ; Benzopyrans/pharmacology ; CHO Cells ; Cell Line, Tumor ; Cricetinae ; Cricetulus ; Disease Models, Animal ; Eukaryotic Initiation Factor-2/metabolism ; HEK293 Cells ; Humans ; Kaplan-Meier Estimate ; Mice ; Phosphorylation/drug effects ; Prion Diseases/drug therapy ; Prion Diseases/metabolism ; Signal Transduction ; Unfolded Protein Response/drug effects ; eIF-2 Kinase/metabolism
Chemical Substances	2-amino-6-chloro-alpha-cyano-3-(ethoxycarbonyl)-4H-1-benzopyran-4-acetic acid ethyl ester ; Acetates ; Benzopyrans ; Eukaryotic Initiation Factor-2 ; PERK kinase (EC 2.7.11.1) ; eIF-2 Kinase (EC 2.7.11.1)
Language	English
Publishing date	2020-08-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.abb4749
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Article ; Online: Restoring Agonist Function at a Chemogenetically Modified M

Khajehali, Elham / Bradley, Sophie / van der Westhuizen, Emma T / Molloy, Colin / Valant, Celine / Finlayson, Lisa / Lindsley, Craig W / Sexton, Patrick M / Tobin, Andrew B / Christopoulos, Arthur

ACS chemical neuroscience

2020 Volume 11, Issue 24, Page(s) 4270–4279

Abstract: Designer receptors exclusively activated by designer drugs (DREADDs) have been successfully employed to activate signaling pathways associated with specific muscarinic acetylcholine receptor (mAChR) subtypes. The ... ...

Abstract	Designer receptors exclusively activated by designer drugs (DREADDs) have been successfully employed to activate signaling pathways associated with specific muscarinic acetylcholine receptor (mAChR) subtypes. The M
MeSH term(s)	Acetylcholine ; Allosteric Regulation ; Animals ; CHO Cells ; Cricetinae ; Cricetulus ; Mice ; Receptor, Muscarinic M1/genetics
Chemical Substances	Receptor, Muscarinic M1 ; Acetylcholine (N9YNS0M02X)
Language	English
Publishing date	2020-11-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1948-7193
ISSN (online)	1948-7193
DOI	10.1021/acschemneuro.0c00540
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Article ; Online: Biased M1 muscarinic receptor mutant mice show accelerated progression of prion neurodegenerative disease.

Scarpa, Miriam / Molloy, Colin / Jenkins, Laura / Strellis, Bethany / Budgett, Rebecca F / Hesse, Sarah / Dwomoh, Louis / Marsango, Sara / Tejeda, Gonzalo S / Rossi, Mario / Ahmed, Zeshan / Milligan, Graeme / Hudson, Brian D / Tobin, Andrew B / Bradley, Sophie J

Proceedings of the National Academy of Sciences of the United States of America

2021 Volume 118, Issue 50

Abstract: There are currently no treatments that can slow the progression of neurodegenerative diseases, such as Alzheimer's disease (AD). There is, however, a growing body of evidence that activation of the M1 muscarinic acetylcholine receptor (M1-receptor) can ... ...

Abstract	There are currently no treatments that can slow the progression of neurodegenerative diseases, such as Alzheimer's disease (AD). There is, however, a growing body of evidence that activation of the M1 muscarinic acetylcholine receptor (M1-receptor) can not only restore memory loss in AD patients but in preclinical animal models can also slow neurodegenerative disease progression. The generation of an effective medicine targeting the M1-receptor has however been severely hampered by associated cholinergic adverse responses. By using genetically engineered mouse models that express a G protein-biased M1-receptor, we recently established that M1-receptor mediated adverse responses can be minimized by ensuring activating ligands maintain receptor phosphorylation/arrestin-dependent signaling. Here, we use these same genetic models in concert with murine prion disease, a terminal neurodegenerative disease showing key hallmarks of AD, to establish that phosphorylation/arrestin-dependent signaling delivers neuroprotection that both extends normal animal behavior and prolongs the life span of prion-diseased mice. Our data point to an important neuroprotective property inherent to the M1-receptor and indicate that next generation M1-receptor ligands designed to drive receptor phosphorylation/arrestin-dependent signaling would potentially show low adverse responses while delivering neuroprotection that will slow disease progression.
MeSH term(s)	Animals ; Cells, Cultured ; GTP-Binding Protein alpha Subunits, Gq-G11/genetics ; GTP-Binding Protein alpha Subunits, Gq-G11/metabolism ; Gene Expression Regulation/physiology ; Mice ; Mice, Knockout ; Neurons/metabolism ; Prion Diseases/genetics ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Receptor, Muscarinic M1/genetics ; Receptor, Muscarinic M1/metabolism ; Signal Transduction
Chemical Substances	Receptor, Muscarinic M1 ; GTP-Binding Protein alpha Subunits, Gq-G11 (EC 3.6.5.1)
Language	English
Publishing date	2021-12-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2107389118
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Article: High-Content Screening and Computational Prediction Reveal Viral Genes That Suppress the Innate Immune Response.

Ng, Tai L / Olson, Erika J / Yoo, Tae Yeon / Weiss, H Sloane / Koide, Yukiye / Koch, Peter D / Rollins, Nathan J / Mach, Pia / Meisinger, Tobias / Bricken, Trenton / Chang, Timothy Z / Molloy, Colin / Zürcher, Jérôme / Chang, Roger L / Mitchison, Timothy J / Glass, John I / Marks, Debora S / Way, Jeffrey C / Silver, Pamela A

mSystems

2022 Volume 7, Issue 2, Page(s) e0146621

Abstract: Suppression of the host innate immune response is a critical aspect of viral replication. Upon infection, viruses may introduce one or more proteins that inhibit key immune pathways, such as the type I interferon pathway. However, the ability to predict ... ...

Abstract	Suppression of the host innate immune response is a critical aspect of viral replication. Upon infection, viruses may introduce one or more proteins that inhibit key immune pathways, such as the type I interferon pathway. However, the ability to predict and evaluate viral protein bioactivity on targeted pathways remains challenging and is typically done on a single-virus or -gene basis. Here, we present a medium-throughput high-content cell-based assay to reveal the immunosuppressive effects of viral proteins. To test the predictive power of our approach, we developed a library of 800 genes encoding known, predicted, and uncharacterized human virus genes. We found that previously known immune suppressors from numerous viral families such as
MeSH term(s)	Humans ; Immunity, Innate ; NF-kappa B ; Immune Evasion ; Viruses/genetics ; Viral Proteins/genetics ; Genes, Viral
Chemical Substances	NF-kappa B ; Viral Proteins
Language	English
Publishing date	2022-03-23
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
ISSN	2379-5077
ISSN	2379-5077
DOI	10.1128/msystems.01466-21
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Article ; Online: Chemogenetics defines receptor-mediated functions of short chain free fatty acids.

Bolognini, Daniele / Barki, Natasja / Butcher, Adrian J / Hudson, Brian D / Sergeev, Eugenia / Molloy, Colin / Moss, Catherine E / Bradley, Sophie J / Le Gouill, Christian / Bouvier, Michel / Tobin, Andrew B / Milligan, Graeme

Nature chemical biology

2019 Volume 15, Issue 5, Page(s) 489–498

Abstract: Differentiating actions of short chain fatty acids (SCFAs) at free fatty acid receptor 2 (FFA2) from other free fatty acid-responsive receptors and from non-receptor-mediated effects has been challenging. Using a novel chemogenetic and knock-in strategy, ...

Abstract	Differentiating actions of short chain fatty acids (SCFAs) at free fatty acid receptor 2 (FFA2) from other free fatty acid-responsive receptors and from non-receptor-mediated effects has been challenging. Using a novel chemogenetic and knock-in strategy, whereby an engineered variant of FFA2 (FFA2-DREADD) that is unresponsive to natural SCFAs but is instead activated by sorbic acid replaced the wild-type receptor, we determined that activation of FFA2 in differentiated adipocytes and colonic crypt enteroendocrine cells of mouse accounts fully for SCFA-regulated lipolysis and release of the incretin glucagon-like peptide-1 (GLP-1), respectively. In vivo studies confirmed the specific role of FFA2 in GLP-1 release and also demonstrated a direct role for FFA2 in accelerating gut transit. Thereby, we establish the general principle that such a chemogenetic knock-in strategy can successfully define novel G-protein-coupled receptor (GPCR) biology and provide both target validation and establish therapeutic potential of a 'hard to target' GPCR.
MeSH term(s)	Animals ; Fatty Acids, Volatile/metabolism ; Humans ; Mice ; Receptors, Cell Surface/chemistry ; Receptors, Cell Surface/genetics ; Receptors, Cell Surface/metabolism ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism
Chemical Substances	FFA2R protein, human ; Fatty Acids, Volatile ; Receptors, Cell Surface ; Receptors, G-Protein-Coupled ; free fatty acid 2 receptor, mouse
Language	English
Publishing date	2019-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/s41589-019-0270-1
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Zs.A 6251: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Biased M1-muscarinic-receptor-mutant mice inform the design of next-generation drugs.

Nature chemical biology

2020 Volume 16, Issue 3, Page(s) 240–249

Abstract: Cholinesterase inhibitors, the current frontline symptomatic treatment for Alzheimer's disease (AD), are associated with low efficacy and adverse effects. M1 muscarinic acetylcholine receptors (M1 mAChRs) represent a potential alternate therapeutic ... ...

Abstract	Cholinesterase inhibitors, the current frontline symptomatic treatment for Alzheimer's disease (AD), are associated with low efficacy and adverse effects. M1 muscarinic acetylcholine receptors (M1 mAChRs) represent a potential alternate therapeutic target; however, drug discovery programs focused on this G protein-coupled receptor (GPCR) have failed, largely due to cholinergic adverse responses. Employing novel chemogenetic and phosphorylation-deficient, G protein-biased, mouse models, paired with a toolbox of probe molecules, we establish previously unappreciated pharmacologically targetable M1 mAChR neurological processes, including anxiety-like behaviors and hyper-locomotion. By mapping the upstream signaling pathways regulating these responses, we determine the importance of receptor phosphorylation-dependent signaling in driving clinically relevant outcomes and in controlling adverse effects including 'epileptic-like' seizures. We conclude that M1 mAChR ligands that promote receptor phosphorylation-dependent signaling would protect against cholinergic adverse effects in addition to driving beneficial responses such as learning and memory and anxiolytic behavior relevant for the treatment of AD.
MeSH term(s)	Acetylcholinesterase/metabolism ; Alzheimer Disease/drug therapy ; Animals ; Cholinergic Agents/pharmacology ; Cholinesterase Inhibitors/metabolism ; Cholinesterase Inhibitors/pharmacology ; Disease Models, Animal ; Drug Design ; Female ; Gene Knock-In Techniques ; Male ; Mice ; Mice, Inbred C57BL ; Phosphorylation ; Receptor, Muscarinic M1/genetics ; Receptor, Muscarinic M1/metabolism
Chemical Substances	Cholinergic Agents ; Cholinesterase Inhibitors ; Receptor, Muscarinic M1 ; Acetylcholinesterase (EC 3.1.1.7)
Language	English
Publishing date	2020-02-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/s41589-019-0453-9
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Article ; Online: Bitopic Binding Mode of an M

Bradley, Sophie J / Molloy, Colin / Bundgaard, Christoffer / Mogg, Adrian J / Thompson, Karen J / Dwomoh, Louis / Sanger, Helen E / Crabtree, Michael D / Brooke, Simon M / Sexton, Patrick M / Felder, Christian C / Christopoulos, Arthur / Broad, Lisa M / Tobin, Andrew B / Langmead, Christopher J

Molecular pharmacology

2018 Volume 93, Issue 6, Page(s) 645–656

Abstract: The realization of the therapeutic potential of targeting the ... ...

Abstract	The realization of the therapeutic potential of targeting the M
MeSH term(s)	Acetylcholine/metabolism ; Allosteric Regulation/drug effects ; Allosteric Site/drug effects ; Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Animals ; Benzimidazoles/pharmacology ; Binding Sites/drug effects ; CHO Cells ; Cell Line ; Clinical Trials as Topic ; Cricetinae ; Cricetulus ; Humans ; Learning/drug effects ; Male ; Memory/drug effects ; Mice ; Mice, Inbred C57BL ; Muscarinic Agonists/pharmacology ; Protein Binding/drug effects ; Rats ; Rats, Wistar ; Receptor, Muscarinic M1/metabolism ; Receptors, Muscarinic/metabolism
Chemical Substances	Benzimidazoles ; GSK 1034702 ; Muscarinic Agonists ; Receptor, Muscarinic M1 ; Receptors, Muscarinic ; benzimidazol-2-one (43135-91-7) ; Acetylcholine (N9YNS0M02X)
Language	English
Publishing date	2018-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	124034-1
ISSN	1521-0111 ; 0026-895X
ISSN (online)	1521-0111
ISSN	0026-895X
DOI	10.1124/mol.118.111872
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Article ; Online: High-content screening of coronavirus genes for innate immune suppression reveals enhanced potency of SARS-CoV-2 proteins

bioRxiv

Abstract: Suppression of the host intracellular innate immune system is an essential aspect of viral replication. Here, we developed a suite of medium-throughput high-content cell-based assays to reveal the effect of individual coronavirus proteins on antiviral ... ...

Abstract	Suppression of the host intracellular innate immune system is an essential aspect of viral replication. Here, we developed a suite of medium-throughput high-content cell-based assays to reveal the effect of individual coronavirus proteins on antiviral innate immune pathways. Using these assays, we screened the 196 protein products of seven coronaviruses (SARS-CoV-2,SARS-CoV-1, 229E, NL63, OC43, HKU1 and MERS). This includes a previously unidentified gene in SARS-CoV-2 encoded within the Spike gene. We observe immune-suppressing activity in both known host-suppressing genes (e.g., NSP1, Orf6, NSP3, and NSP5) as well as other coronavirus genes, including the newly identified SARS-CoV-2 protein. Moreover, the genes encoded by SARS-CoV-2 are generally more potent immune suppressors than their homologues from the other coronaviruses. This suite of pathway-based and mechanism-agnostic assays could serve as the basis for rapid in vitro prediction of the pathogenicity of novel viruses based on provision of sequence information alone.
Keywords	covid19
Language	English
Publishing date	2021-03-02
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.03.02.433434
Database	COVID19

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Article ; Online: RBM3 mediates structural plasticity and protective effects of cooling in neurodegeneration.

Peretti, Diego / Bastide, Amandine / Radford, Helois / Verity, Nicholas / Molloy, Colin / Martin, Maria Guerra / Moreno, Julie A / Steinert, Joern R / Smith, Tim / Dinsdale, David / Willis, Anne E / Mallucci, Giovanna R

Nature

2015 Volume 518, Issue 7538, Page(s) 236–239

Abstract: In the healthy adult brain synapses are continuously remodelled through a process of elimination and formation known as structural plasticity. Reduction in synapse number is a consistent early feature of neurodegenerative diseases, suggesting deficient ... ...

Abstract	In the healthy adult brain synapses are continuously remodelled through a process of elimination and formation known as structural plasticity. Reduction in synapse number is a consistent early feature of neurodegenerative diseases, suggesting deficient compensatory mechanisms. Although much is known about toxic processes leading to synaptic dysfunction and loss in these disorders, how synaptic regeneration is affected is unknown. In hibernating mammals, cooling induces loss of synaptic contacts, which are reformed on rewarming, a form of structural plasticity. We have found that similar changes occur in artificially cooled laboratory rodents. Cooling and hibernation also induce a number of cold-shock proteins in the brain, including the RNA binding protein, RBM3 (ref. 6). The relationship of such proteins to structural plasticity is unknown. Here we show that synapse regeneration is impaired in mouse models of neurodegenerative disease, in association with the failure to induce RBM3. In both prion-infected and 5XFAD (Alzheimer-type) mice, the capacity to regenerate synapses after cooling declined in parallel with the loss of induction of RBM3. Enhanced expression of RBM3 in the hippocampus prevented this deficit and restored the capacity for synapse reassembly after cooling. RBM3 overexpression, achieved either by boosting endogenous levels through hypothermia before the loss of the RBM3 response or by lentiviral delivery, resulted in sustained synaptic protection in 5XFAD mice and throughout the course of prion disease, preventing behavioural deficits and neuronal loss and significantly prolonging survival. In contrast, knockdown of RBM3 exacerbated synapse loss in both models and accelerated disease and prevented the neuroprotective effects of cooling. Thus, deficient synapse regeneration, mediated at least in part by failure of the RBM3 stress response, contributes to synapse loss throughout the course of neurodegenerative disease. The data support enhancing cold-shock pathways as potential protective therapies in neurodegenerative disorders.
MeSH term(s)	Alzheimer Disease/metabolism ; Animals ; Cold Shock Proteins and Peptides/metabolism ; Cold Temperature ; Cold-Shock Response/physiology ; Disease Models, Animal ; Hibernation/physiology ; Hippocampus/metabolism ; Male ; Mice ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neuronal Plasticity ; Neuroprotective Agents ; Prions/physiology ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Regeneration ; Synapses/metabolism
Chemical Substances	Cold Shock Proteins and Peptides ; Neuroprotective Agents ; Prions ; RNA-Binding Proteins ; Rbm3 protein, mouse
Language	English
Publishing date	2015-01-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature14142
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