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Article ; Online: Sodium regulates PLC and IP

James, Andrew D / Unthank, Katherine P / Jones, Isobel / Sajjaboontawee, Nattanan / Sizer, Rebecca E / Chawla, Sangeeta / Evans, Gareth J O / Brackenbury, William J

Physiological reports

2023 Volume 11, Issue 7, Page(s) e15663

Abstract: Intracellular ... ...

Abstract	Intracellular Ca
MeSH term(s)	Humans ; Female ; Calcium Signaling/physiology ; Sodium/metabolism ; Sodium-Calcium Exchanger/metabolism ; Breast Neoplasms ; Ion Channels/metabolism ; Calcium/metabolism
Chemical Substances	Sodium (9NEZ333N27) ; Sodium-Calcium Exchanger ; Ion Channels ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2023-04-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2724325-4
ISSN	2051-817X ; 2051-817X
ISSN (online)	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.15663
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The phosphatase Glc7 controls the eisosomal response to starvation via post-translational modification of Pil1.

Paine, Katherine M / Laidlaw, Kamilla M E / Evans, Gareth J O / MacDonald, Chris

Journal of cell science

2023 Volume 136, Issue 14

Abstract: The yeast (Saccharomyces cerevisiae) plasma membrane (PM) is organised into specific subdomains that regulate surface membrane proteins. Surface transporters actively uptake nutrients in particular regions of the PM where they are also susceptible to ... ...

Abstract	The yeast (Saccharomyces cerevisiae) plasma membrane (PM) is organised into specific subdomains that regulate surface membrane proteins. Surface transporters actively uptake nutrients in particular regions of the PM where they are also susceptible to substrate-induced endocytosis. However, transporters also diffuse into distinct subdomains termed eisosomes, where they are protected from endocytosis. Although most nutrient transporter populations are downregulated in the vacuole following glucose starvation, a small pool is retained in eisosomes to provide efficient recovery from starvation. We find the core eisosome subunit Pil1, a Bin, Amphiphysin and Rvs (BAR) domain protein required for eisosome biogenesis, is phosphorylated primarily by the kinase Pkh2. In response to acute glucose starvation, Pil1 is rapidly dephosphorylated. Enzyme localisation and activity screens suggest that the phosphatase Glc7 is the primary enzyme responsible for Pil1 dephosphorylation. Defects in Pil1 phosphorylation, achieved by depletion of GLC7 or expression of phospho-ablative or phospho-mimetic mutants, correlate with reduced retention of transporters in eisosomes and inefficient starvation recovery. We propose that precise post-translational control of Pil1 modulates nutrient transporter retention within eisosomes, depending on extracellular nutrient levels, to maximise recovery following starvation.
MeSH term(s)	Saccharomyces cerevisiae Proteins/metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Cell Membrane/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Protein Processing, Post-Translational ; Glucose/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; Membrane Proteins ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2023-07-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.260505
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Article ; Online: The synaptosome as a model system for studying synaptic physiology.

Evans, Gareth J O

Cold Spring Harbor protocols

2015 Volume 2015, Issue 5, Page(s) 421–424

Abstract: Alongside rodent brain slices and primary neuronal cultures, synaptosomes (isolated nerve terminals) have been an important model system for studying the molecular mechanisms of synaptic function in the brain. Synaptosomes were first prepared in the late ...

Abstract	Alongside rodent brain slices and primary neuronal cultures, synaptosomes (isolated nerve terminals) have been an important model system for studying the molecular mechanisms of synaptic function in the brain. Synaptosomes were first prepared in the late 1950s by Whittaker and colleagues and were instrumental in studying synaptic structure and defining the functional components of the synapse, including the identity of the major neurotransmitters and their uptake mechanisms. Synaptosomes can also be stimulated to release neurotransmitters and were used to discover a number of regulatory signaling pathways that fine-tune synaptic transmission. In the past decade, landmark proteomic studies of synaptosomes and synaptic vesicle preparations have further dissected the protein composition of the synapse. This introduction briefly describes the history of the synaptosome preparation and highlights how it continues to be relevant as our focus in the neuroscience community centers on synaptic dysfunction in aging and neurological disease.
MeSH term(s)	Animals ; Brain/physiology ; Cell Fractionation/methods ; Chromosome Pairing/physiology ; Models, Biological ; Rodentia ; Synaptosomes/metabolism
Language	English
Publishing date	2015-05-01
Publishing country	United States
Document type	Journal Article
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.top074450
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Article ; Online: Subcellular fractionation of the brain: preparation of synaptosomes and synaptic vesicles.

Evans, Gareth J O

Cold Spring Harbor protocols

2015 Volume 2015, Issue 5, Page(s) 462–466

Abstract: The human brain is estimated to contain trillions of synaptic nerve terminals. These are the connections between neurons that are responsible for transmitting information and are modified as a result of learning. A valuable tool for studying synapses is ... ...

Abstract	The human brain is estimated to contain trillions of synaptic nerve terminals. These are the connections between neurons that are responsible for transmitting information and are modified as a result of learning. A valuable tool for studying synapses is the isolated nerve terminal, or synaptosome, which is obtained by homogenizing the brain in such a way that individual synapses pinch off to form metabolically active compartments that can recapitulate neurotransmitter release. This protocol describes the stepwise fractionation of rat brain tissue to yield synaptosomes and synaptic vesicles, which can be used in many different experimental approaches to study the structure and protein composition of the synapse and even dissect the molecular mechanisms of neurotransmission.
MeSH term(s)	Animals ; Brain/cytology ; Brain Chemistry ; Cell Fractionation/methods ; Rats ; Synaptic Vesicles/chemistry ; Synaptic Vesicles/metabolism ; Synaptic Vesicles/physiology ; Synaptosomes/chemistry ; Synaptosomes/metabolism ; Synaptosomes/physiology
Language	English
Publishing date	2015-05-01
Publishing country	United States
Document type	Journal Article
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.prot083469
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Article: Degradation of silicon photonic biosensors in cell culture media: analysis and prevention.

Triggs, Graham J / Evans, Gareth J O / Krauss, Thomas F

Biomedical optics express

2017 Volume 8, Issue 6, Page(s) 2924–2931

Abstract: Silicon photonic biosensors are being widely researched as they combine high performance with the potential for low-cost mass-manufacturing. Sensing is typically performed in an aqueous environment and it is assumed that the sensor is chemically stable, ... ...

Abstract	Silicon photonic biosensors are being widely researched as they combine high performance with the potential for low-cost mass-manufacturing. Sensing is typically performed in an aqueous environment and it is assumed that the sensor is chemically stable, as silicon is known to etch in strong alkaline solutions but not in liquids with a pH close to 7. Here, we show that silicon can be affected surprisingly strongly by typical cell culture media, and we observe etch rates of up to 2 nm/hour. We then demonstrate that a very thin (< 10 nm) layer of thermal oxide is sufficient to suppress the etching process and provide the long-term stability required for monitoring cells and related biological processes over extended periods of time. We also show that employing an additional pH buffering compound in the culture medium can significantly reduce the etch rate.
Language	English
Publishing date	2017-05-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	2572216-5
ISSN	2156-7085
ISSN	2156-7085
DOI	10.1364/BOE.8.002924
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Article ; Online: JNK signalling regulates antioxidant responses in neurons.

Ugbode, Chris / Garnham, Nathan / Fort-Aznar, Laura / Evans, Gareth J O / Chawla, Sangeeta / Sweeney, Sean T

Redox biology

2020 Volume 37, Page(s) 101712

Abstract: Reactive oxygen species (ROS) are generated during physiological bouts of synaptic activity and as a consequence of pathological conditions in the central nervous system. How neurons respond to and distinguish between ROS in these different contexts is ... ...

Abstract	Reactive oxygen species (ROS) are generated during physiological bouts of synaptic activity and as a consequence of pathological conditions in the central nervous system. How neurons respond to and distinguish between ROS in these different contexts is currently unknown. In Drosophila mutants with enhanced JNK activity, lower levels of ROS are observed and these animals are resistant to both changes in ROS and changes in synapse morphology induced by oxidative stress. In wild type flies, disrupting JNK-AP-1 signalling perturbs redox homeostasis suggesting JNK activity positively regulates neuronal antioxidant defense. We validated this hypothesis in mammalian neurons, finding that JNK activity regulates the expression of the antioxidant gene Srxn-1, in a c-Jun dependent manner. We describe a conserved 'adaptive' role for neuronal JNK in the maintenance of redox homeostasis that is relevant to several neurodegenerative diseases.
MeSH term(s)	Animals ; Antioxidants ; JNK Mitogen-Activated Protein Kinases/genetics ; JNK Mitogen-Activated Protein Kinases/metabolism ; MAP Kinase Signaling System ; Neurons/metabolism ; Oxidative Stress ; Reactive Oxygen Species
Chemical Substances	Antioxidants ; Reactive Oxygen Species ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2020-09-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2020.101712
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Article ; Online: Amyloid-β oligomerization monitored by single-molecule stepwise photobleaching.

Dresser, Lara / Hunter, Patrick / Yendybayeva, Fatima / Hargreaves, Alex L / Howard, Jamieson A L / Evans, Gareth J O / Leake, Mark C / Quinn, Steven D

Methods (San Diego, Calif.)

2020 Volume 193, Page(s) 80–95

Abstract: A major hallmark of Alzheimer's disease is the misfolding and aggregation of the amyloid- β peptide (Aβ). While early research pointed towards large fibrillar- and plaque-like aggregates as being the most toxic species, recent evidence now implicates ... ...

Abstract	A major hallmark of Alzheimer's disease is the misfolding and aggregation of the amyloid- β peptide (Aβ). While early research pointed towards large fibrillar- and plaque-like aggregates as being the most toxic species, recent evidence now implicates small soluble Aβ oligomers as being orders of magnitude more harmful. Techniques capable of characterizing oligomer stoichiometry and assembly are thus critical for a deeper understanding of the earliest stages of neurodegeneration and for rationally testing next-generation oligomer inhibitors. While the fluorescence response of extrinsic fluorescent probes such as Thioflavin-T have become workhorse tools for characterizing large Aβ aggregates in solution, it is widely accepted that these methods suffer from many important drawbacks, including an insensitivity to oligomeric species. Here, we integrate several biophysics techniques to gain new insight into oligomer formation at the single-molecule level. We showcase single-molecule stepwise photobleaching of fluorescent dye molecules as a powerful method to bypass many of the traditional limitations, and provide a step-by-step guide to implementing the technique in vitro. By collecting fluorescence emission from single Aβ(1-42) peptides labelled at the N-terminal position with HiLyte Fluor 555 via wide-field total internal reflection fluorescence (TIRF) imaging, we demonstrate how to characterize the number of peptides per single immobile oligomer and reveal heterogeneity within sample populations. Importantly, fluorescence emerging from Aβ oligomers cannot be easily investigated using diffraction-limited optical microscopy tools. To assay oligomer activity, we also demonstrate the implementation of another biophysical method involving the ratiometric imaging of Fura-2-AM loaded cells which quantifies the rate of oligomer-induced dysregulation of intracellular Ca
MeSH term(s)	Alzheimer Disease ; Amyloid beta-Peptides ; Fluorescent Dyes ; Humans ; Peptide Fragments ; Photobleaching ; Protein Aggregates
Chemical Substances	Amyloid beta-Peptides ; Fluorescent Dyes ; Peptide Fragments ; Protein Aggregates
Language	English
Publishing date	2020-06-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2020.06.007
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Zs.A 3239: Show issues

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Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: N1-Src Kinase Is Required for Primary Neurogenesis in

Lewis, Philip A / Bradley, Isobel C / Pizzey, Alastair R / Isaacs, Harry V / Evans, Gareth J O

The Journal of neuroscience : the official journal of the Society for Neuroscience

2017 Volume 37, Issue 35, Page(s) 8477–8485

Abstract: The presence of the neuronal-specific N1-Src splice variant of the C-Src tyrosine kinase is conserved through vertebrate evolution, suggesting an important role in complex nervous systems. Alternative splicing involving ... ...

Abstract	The presence of the neuronal-specific N1-Src splice variant of the C-Src tyrosine kinase is conserved through vertebrate evolution, suggesting an important role in complex nervous systems. Alternative splicing involving an
MeSH term(s)	Animals ; Cell Differentiation/physiology ; Enzyme Activation ; Male ; Neural Stem Cells/cytology ; Neural Stem Cells/enzymology ; Neurogenesis/physiology ; Neurons/cytology ; Neurons/enzymology ; Protein Isoforms ; Xenopus/anatomy & histology ; Xenopus/physiology ; src-Family Kinases/genetics ; src-Family Kinases/metabolism
Chemical Substances	Protein Isoforms ; src-Family Kinases (EC 2.7.10.2)
Language	English
Publishing date	2017-08-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.3881-16.2017
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Zs.A 1668: Show issues

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Article ; Online: Synaptic signalling in cerebellar plasticity.

Evans, Gareth J O

Biology of the cell

2007 Volume 99, Issue 7, Page(s) 363–378

Abstract: A major goal of learning and memory research is to correlate the function of molecules with the behaviour of organisms. The beautiful laminar structure of the cerebellar cortex lends itself to the study of synaptic plasticity, because its clearly defined ...

Abstract	A major goal of learning and memory research is to correlate the function of molecules with the behaviour of organisms. The beautiful laminar structure of the cerebellar cortex lends itself to the study of synaptic plasticity, because its clearly defined patterns of neurons and their synapses form circuits that have been implicated in simple motor behaviour paradigms. The best understood in terms of molecular mechanism is the parallel fibre-Purkinje cell synapse, where presynaptic long-term potentiation and postsynaptic long-term depression and potentiation finely tune cerebellar output. Our understanding of these forms of plasticity has mostly come from the electrophysiological and behavioural analysis of knockout mutant mice, but more recently the knock-in of synaptic molecules with mutated phosphorylation sites and binding domains has provided more detailed insights into the signalling events. The present review details the major forms of plasticity in the cerebellar cortex, with particular attention to the membrane trafficking and intracellular signalling responsible. This overview of the current literature suggests it will not be long before the involvement of the cerebellum in certain motor behaviours is fully explained in molecular terms.
MeSH term(s)	Animals ; Behavior/physiology ; Cerebellar Cortex/cytology ; Cerebellar Cortex/physiology ; Long-Term Potentiation/physiology ; Long-Term Synaptic Depression/physiology ; Memory/physiology ; Nerve Fibers/metabolism ; Neuronal Plasticity/physiology ; Signal Transduction/physiology ; Synapses/physiology ; Synaptic Transmission/physiology
Language	English
Publishing date	2007-07
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1042/BC20070010
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Zs.A 758: Show issues

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Article: Amyloid-β oligomerization monitored by single-molecule stepwise photobleaching

Dresser, Lara / Hunter, Patrick / Yendybayeva, Fatima / Hargreaves, Alex L / Howard, Jamieson A.L / Evans, Gareth J.O / Leake, Mark C / Quinn, Steven D

Methods. 2020 June 10,

2020

Abstract: A major hallmark of Alzheimer’s disease is the misfolding and aggregation of the amyloid- β peptide (Aβ). While early research pointed towards large fibrillar- and plaque-like aggregates as being the most toxic species, recent evidence now implicates ... ...

Abstract	A major hallmark of Alzheimer’s disease is the misfolding and aggregation of the amyloid- β peptide (Aβ). While early research pointed towards large fibrillar- and plaque-like aggregates as being the most toxic species, recent evidence now implicates small soluble Aβ oligomers as being orders of magnitude more harmful. Techniques capable of characterizing oligomer stoichiometry and assembly are thus critical for a deeper understanding of the earliest stages of neurodegeneration and for rationally testing next-generation oligomer inhibitors. While the fluorescence response of extrinsic fluorescent probes such as Thioflavin-T have become workhorse tools for characterizing large Aβ aggregates in solution, it is widely accepted that these methods suffer from many important drawbacks, including an insensitivity to oligomeric species. Here, we integrate several biophysics techniques to gain new insight into oligomer formation at the single-molecule level. We showcase single-molecule stepwise photobleaching of fluorescent dye molecules as a powerful method to bypass many of the traditional limitations, and provide a step-by-step guide to implementing the technique in vitro. By collecting fluorescence emission from single Aβ(1–42) peptides labelled at the N-terminal position with HiLyte Fluor 555 via wide-field total internal reflection fluorescence (TIRF) imaging, we demonstrate how to characterize the number of peptides per single immobile oligomer and reveal heterogeneity within sample populations. Importantly, fluorescence emerging from Aβ oligomers cannot be easily investigated using diffraction-limited optical microscopy tools. To assay oligomer activity, we also demonstrate the implementation of another biophysical method involving the ratiometric imaging of Fura-2-AM loaded cells which quantifies the rate of oligomer-induced dysregulation of intracellular Ca²⁺ homeostasis. We anticipate that the integrated single-molecule biophysics approaches highlighted here will develop further and in principle may be extended to the investigation of other protein aggregation systems under controlled experimental conditions.
Keywords	Alzheimer disease ; amyloid ; biophysics ; calcium ; fluorescence ; fluorescent dyes ; homeostasis ; image analysis ; light microscopy ; neurodegenerative diseases ; oligomerization ; peptides ; photobleaching ; stoichiometry ; toxicity
Language	English
Dates of publication	2020-0610
Publishing place	Elsevier Inc.
Document type	Article
Note	Pre-press version
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2020.06.007
Database	NAL-Catalogue (AGRICOLA)

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