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Article ; Online: Oxidation modulates LINGO2-induced inactivation of large conductance, Ca

Dudem, Srikanth / Boon, Pei Xin / Mullins, Nicholas / McClafferty, Heather / Shipston, Michael J / Wilkinson, Richard D A / Lobb, Ian / Sergeant, Gerard P / Thornbury, Keith D / Tikhonova, Irina G / Hollywood, Mark A

The Journal of biological chemistry

2023 Volume 299, Issue 3, Page(s) 102975

Abstract: ... ...

Abstract	Ca
MeSH term(s)	Large-Conductance Calcium-Activated Potassium Channels/genetics ; Large-Conductance Calcium-Activated Potassium Channels/metabolism ; Cysteine/metabolism ; Oxidation-Reduction ; Peptides/metabolism ; Methionine/metabolism ; Calcium/metabolism
Chemical Substances	Large-Conductance Calcium-Activated Potassium Channels ; Cysteine (K848JZ4886) ; Peptides ; Methionine (AE28F7PNPL) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2023-02-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.102975
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Article ; Online: The malaria parasite chaperonin containing TCP-1 (CCT) complex

Mark D. Wilkinson / Josie L. Ferreira / Morgan Beeby / Jake Baum / Keith R. Willison

Frontiers in Molecular Biosciences, Vol

Data integration with other CCT proteomes

2022 Volume 9

Abstract: The multi-subunit chaperonin containing TCP-1 (CCT) is an essential molecular chaperone that functions in the folding of key cellular proteins. This paper reviews the interactome of the eukaryotic chaperonin CCT and its primary clients, the ubiquitous ... ...

Abstract	The multi-subunit chaperonin containing TCP-1 (CCT) is an essential molecular chaperone that functions in the folding of key cellular proteins. This paper reviews the interactome of the eukaryotic chaperonin CCT and its primary clients, the ubiquitous cytoskeletal proteins, actin and tubulin. CCT interacts with other nascent proteins, especially the WD40 propeller proteins, and also assists in the assembly of several protein complexes. A new proteomic dataset is presented for CCT purified from the human malarial parasite, P. falciparum (PfCCT). The CCT8 subunit gene was C-terminally FLAG-tagged using Selection Linked Integration (SLI) and CCT complexes were extracted from infected human erythrocyte cultures synchronized for maximum expression levels of CCT at the trophozoite stage of the parasite’s asexual life cycle. We analyze the new PfCCT proteome and incorporate it into our existing model of the CCT system, supported by accumulated data from biochemical and cell biological experiments in many eukaryotic species. Together with measurements of CCT mRNA, CCT protein subunit copy number and the post-translational and chemical modifications of the CCT subunits themselves, a cumulative picture is emerging of an essential molecular chaperone system sitting at the heart of eukaryotic cell growth control and cell cycle regulation.
Keywords	chaperonin ; P. falciparum ; autophagy ; WD40 propellors ; cytoskeleton ; protein coacervate ; Biology (General) ; QH301-705.5
Subject code	612
Language	English
Publishing date	2022-12-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
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Article ; Online: Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.

Chernova, Tatiana A / Chernoff, Yury O / Wilkinson, Keith D

Molecules (Basel, Switzerland)

2019 Volume 24, Issue 18

Abstract: Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature). Prion features were recently reported for various proteins involved in amyloid and ... ...

Abstract	Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature). Prion features were recently reported for various proteins involved in amyloid and neural inclusion disorders. Heritable yeast prions share molecular properties (and in the case of polyglutamines, amino acid composition) with human disease-related amyloids. Fundamental protein quality control pathways, including chaperones, the ubiquitin proteasome system and autophagy are highly conserved between yeast and human cells. Crucial cellular proteins and conditions influencing amyloids and prions were uncovered in the yeast model. The treatments available for neurodegenerative amyloid-associated diseases are few and their efficiency is limited. Yeast models of amyloid-related neurodegenerative diseases have become powerful tools for high-throughput screening for chemical compounds and FDA-approved drugs that reduce aggregation and toxicity of amyloids. Although some environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. Environmental stresses trigger amyloid formation and loss, acting either via influencing intracellular concentrations of the amyloidogenic proteins or via heterologous inducers of prions. Studies of environmental and physiological regulation of yeast prions open new possibilities for pharmacological intervention and/or prophylactic procedures aiming on common cellular systems rather than the properties of specific amyloids.
MeSH term(s)	Amyloid/metabolism ; Animals ; Fungal Proteins/metabolism ; Humans ; Models, Biological ; Neurodegenerative Diseases/metabolism ; Yeasts/metabolism
Chemical Substances	Amyloid ; Fungal Proteins
Language	English
Publishing date	2019-09-18
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules24183388
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Article: A focused update to the 2019 NLA scientific statement on use of lipoprotein(a) in clinical practice.

Koschinsky, Marlys L / Bajaj, Archna / Boffa, Michael B / Dixon, Dave L / Ferdinand, Keith C / Gidding, Samuel S / Gill, Edward A / Jacobson, Terry A / Michos, Erin D / Safarova, Maya S / Soffer, Daniel E / Taub, Pam R / Wilkinson, Michael J / Wilson, Don P / Ballantyne, Christie M

Journal of clinical lipidology

2024

Abstract: Since the 2019 National Lipid Association (NLA) Scientific Statement on Use of Lipoprotein(a) in Clinical Practice was issued, accumulating epidemiological data have clarified the relationship between lipoprotein(a) [Lp(a)] level and cardiovascular ... ...

Abstract	Since the 2019 National Lipid Association (NLA) Scientific Statement on Use of Lipoprotein(a) in Clinical Practice was issued, accumulating epidemiological data have clarified the relationship between lipoprotein(a) [Lp(a)] level and cardiovascular disease risk and risk reduction. Therefore, the NLA developed this focused update to guide clinicians in applying this emerging evidence in clinical practice. We now have sufficient evidence to support the recommendation to measure Lp(a) levels at least once in every adult for risk stratification. Individuals with Lp(a) levels <75 nmol/L (30 mg/dL) are considered low risk, individuals with Lp(a) levels ≥125 nmol/L (50 mg/dL) are considered high risk, and individuals with Lp(a) levels between 75 and 125 nmol/L (30-50 mg/dL) are at intermediate risk. Cascade screening of first-degree relatives of patients with elevated Lp(a) can identify additional individuals at risk who require intervention. Patients with elevated Lp(a) should receive early, more-intensive risk factor management, including lifestyle modification and lipid-lowering drug therapy in high-risk individuals, primarily to reduce low-density lipoprotein cholesterol (LDL-C) levels. The U.S. Food and Drug Administration approved an indication for lipoprotein apheresis (which reduces both Lp(a) and LDL-C) in high-risk patients with familial hypercholesterolemia and documented coronary or peripheral artery disease whose Lp(a) level remains ≥60 mg/dL [∼150 nmol/L)] and LDL-C ≥ 100 mg/dL on maximally tolerated lipid-lowering therapy. Although Lp(a) is an established independent causal risk factor for cardiovascular disease, and despite the high prevalence of Lp(a) elevation (∼1 of 5 individuals), measurement rates are low, warranting improved screening strategies for cardiovascular disease prevention.
Language	English
Publishing date	2024-03-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2365061-8
ISSN	1876-4789 ; 1933-2874
ISSN (online)	1876-4789
ISSN	1933-2874
DOI	10.1016/j.jacl.2024.03.001
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Article ; Online: Quantitative analysis of protein-protein interactions.

Eletr, Ziad M / Wilkinson, Keith D

Methods in molecular biology (Clifton, N.J.)

2015 Volume 1278, Page(s) 23–37

Abstract: Numerous authors, including contributors to this volume, have described methods to detect protein-protein interactions. Many of these approaches are now accessible to the inexperienced investigator thanks to core facilities and/or affordable ... ...

Abstract	Numerous authors, including contributors to this volume, have described methods to detect protein-protein interactions. Many of these approaches are now accessible to the inexperienced investigator thanks to core facilities and/or affordable instrumentation. This chapter discusses some common design considerations that are necessary to obtain valid measurements, as well as the assumptions and analytical methods that are relevant to the quantitation of these interactions.
MeSH term(s)	Binding Sites ; Crystallography, X-Ray ; Ligands ; Molecular Biology/methods ; Protein Binding ; Protein Interaction Maps ; Proteins/chemistry ; Proteins/metabolism
Chemical Substances	Ligands ; Proteins
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-2425-7_2
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Article: Correction: Single-molecule nanopore sensing of actin dynamics and drug binding.

Wang, Xiaoyi / Wilkinson, Mark D / Lin, Xiaoyan / Ren, Ren / Willison, Keith R / Ivanov, Aleksandar P / Baum, Jake / Edel, Joshua B

Chemical science

2020 Volume 11, Issue 30, Page(s) 8036–8038

Abstract: This corrects the article DOI: 10.1039/C9SC05710B.]. ...

Abstract	[This corrects the article DOI: 10.1039/C9SC05710B.].
Language	English
Publishing date	2020-07-23
Publishing country	England
Document type	Published Erratum
ZDB-ID	2559110-1
ISSN	2041-6539 ; 2041-6520
ISSN (online)	2041-6539
ISSN	2041-6520
DOI	10.1039/d0sc90132f
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Article: DUBs at a glance.

Wilkinson, Keith D

Journal of cell science

2009 Volume 122, Issue Pt 14, Page(s) 2325–2329

MeSH term(s)	Animals ; Bacterial Infections/metabolism ; Endopeptidases/metabolism ; Humans ; Immediate-Early Proteins/metabolism ; Neoplasms/metabolism ; Nervous System Diseases/metabolism ; Protein Processing, Post-Translational ; Signal Transduction/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Ubiquitins/genetics ; Ubiquitins/metabolism
Chemical Substances	Immediate-Early Proteins ; Ubiquitins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Endopeptidases (EC 3.4.-)
Keywords	covid19
Language	English
Publishing date	2009-07-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.041046
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Zs.MG 14: Show issues

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Article ; Online: Prions, Chaperones, and Proteostasis in Yeast.

Chernova, Tatiana A / Wilkinson, Keith D / Chernoff, Yury O

Cold Spring Harbor perspectives in biology

2017 Volume 9, Issue 2

Abstract: Prions are alternatively folded, self-perpetuating protein isoforms involved in a variety of biological and pathological processes. Yeast prions are protein-based heritable elements that serve as an excellent experimental system for studying prion ... ...

Abstract	Prions are alternatively folded, self-perpetuating protein isoforms involved in a variety of biological and pathological processes. Yeast prions are protein-based heritable elements that serve as an excellent experimental system for studying prion biology. The propagation of yeast prions is controlled by the same Hsp104/70/40 chaperone machinery that is involved in the protection of yeast cells against proteotoxic stress. Ribosome-associated chaperones, proteolytic pathways, cellular quality-control compartments, and cytoskeletal networks influence prion formation, maintenance, and toxicity. Environmental stresses lead to asymmetric prion distribution in cell divisions. Chaperones and cytoskeletal proteins mediate this effect. Overall, this is an intimate relationship with the protein quality-control machinery of the cell, which enables prions to be maintained and reproduced. The presence of many of these same mechanisms in higher eukaryotes has implications for the diagnosis and treatment of mammalian amyloid diseases.
MeSH term(s)	Heat-Shock Proteins/metabolism ; Molecular Chaperones/metabolism ; Prions ; Yeasts/metabolism
Chemical Substances	Heat-Shock Proteins ; Molecular Chaperones ; Prions
Language	English
Publishing date	2017-02-01
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a023663
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Article ; Online: Yeast Models for Amyloids and Prions

Tatiana A. Chernova / Yury O. Chernoff / Keith D. Wilkinson

Molecules, Vol 24, Iss 18, p

Environmental Modulation and Drug Discovery

2019 Volume 3388

Abstract	Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature). Prion features were recently reported for various proteins involved in amyloid and neural inclusion disorders. Heritable yeast prions share molecular properties (and in the case of polyglutamines, amino acid composition) with human disease-related amyloids. Fundamental protein quality control pathways, including chaperones, the ubiquitin proteasome system and autophagy are highly conserved between yeast and human cells. Crucial cellular proteins and conditions influencing amyloids and prions were uncovered in the yeast model. The treatments available for neurodegenerative amyloid-associated diseases are few and their efficiency is limited. Yeast models of amyloid-related neurodegenerative diseases have become powerful tools for high-throughput screening for chemical compounds and FDA-approved drugs that reduce aggregation and toxicity of amyloids. Although some environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. Environmental stresses trigger amyloid formation and loss, acting either via influencing intracellular concentrations of the amyloidogenic proteins or via heterologous inducers of prions. Studies of environmental and physiological regulation of yeast prions open new possibilities for pharmacological intervention and/or prophylactic procedures aiming on common cellular systems rather than the properties of specific amyloids.
Keywords	amyloid ; prion ; chaperone ; ubiquitin ; heat shock ; environmental factors ; neurodegenerative disease ; drug discovery ; Organic chemistry ; QD241-441
Subject code	570
Language	English
Publishing date	2019-09-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Prion-based memory of heat stress in yeast.

Chernova, Tatiana A / Chernoff, Yury O / Wilkinson, Keith D

Prion

2017 Volume 11, Issue 3, Page(s) 151–161

Abstract: Amyloids and amyloid-based prions are self-perpetuating protein aggregates which can spread by converting a normal protein of the same sequence into a prion form. They are associated with diseases in humans and mammals, and control heritable traits in ... ...

Abstract	Amyloids and amyloid-based prions are self-perpetuating protein aggregates which can spread by converting a normal protein of the same sequence into a prion form. They are associated with diseases in humans and mammals, and control heritable traits in yeast and other fungi. Some amyloids are implicated in biologically beneficial processes. As prion formation generates reproducible memory of a conformational change, prions can be considered as molecular memory devices. We have demonstrated that in yeast, stress-inducible cytoskeleton-associated protein Lsb2 forms a metastable prion in response to high temperature. This prion promotes conversion of other proteins into prions and can persist in a fraction of cells for a significant number of cell generations after stress, thus maintaining the memory of stress in a population of surviving cells. Acquisition of an amino acid substitution required for Lsb2 to form a prion coincides with acquisition of increased thermotolerance in the evolution of Saccharomyces yeast. Thus the ability to form an Lsb2 prion in response to stress coincides with yeast adaptation to growth at higher temperatures. These findings intimately connect prion formation to the cellular response to environmental stresses.
MeSH term(s)	Amino Acid Sequence ; Environment ; Heat-Shock Response ; Hot Temperature ; Peptide Termination Factors/genetics ; Peptide Termination Factors/metabolism ; Prions/genetics ; Prions/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Homology ; Stress, Physiological
Chemical Substances	Peptide Termination Factors ; Prions ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2017-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1933-690X
ISSN (online)	1933-690X
DOI	10.1080/19336896.2017.1328342
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