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  1. Artikel ; Online: Marveling at the Incredible ULK4.

    Eyers, Patrick A

    Structure (London, England : 1993)

    2020  Band 28, Heft 11, Seite(n) 1181–1183

    Abstract: Unc-51-like kinase 4 (ULK4) is a pseudokinase conserved in most eukaryotes, yet ULK4 signaling mechanisms remain enigmatic. In this issue of Structure, Preuss and colleagues report a structure of the ATP-bound ULK4 pseudokinase domain, supported by ... ...

    Abstract Unc-51-like kinase 4 (ULK4) is a pseudokinase conserved in most eukaryotes, yet ULK4 signaling mechanisms remain enigmatic. In this issue of Structure, Preuss and colleagues report a structure of the ATP-bound ULK4 pseudokinase domain, supported by proteomic analysis of the ULK4 interactome and in-depth evolutionary analysis of the intriguingULK4 pseudokinase domain.
    Mesh-Begriff(e) Nucleotides ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Proteomics ; Signal Transduction
    Chemische Substanzen Nucleotides ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Sprache Englisch
    Erscheinungsdatum 2020-10-27
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Comment
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2020.10.005
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  2. Artikel ; Online: A new consensus for evaluating CDKL5/STK9-dependent signalling mechanisms.

    Eyers, Patrick A

    The EMBO journal

    2018  Band 37, Heft 24

    Mesh-Begriff(e) Animals ; Epileptic Syndromes/genetics ; Epileptic Syndromes/metabolism ; Epileptic Syndromes/pathology ; Humans ; Microtubules/genetics ; Microtubules/metabolism ; Phosphorylation/genetics ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction ; Spasms, Infantile/genetics ; Spasms, Infantile/metabolism ; Spasms, Infantile/pathology
    Chemische Substanzen Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; CDKL5 protein, human (EC 2.7.11.22)
    Sprache Englisch
    Erscheinungsdatum 2018-10-30
    Erscheinungsland England
    Dokumenttyp Journal Article ; Review
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2018100848
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  3. Artikel ; Online: Back to the future: new target-validated Rab antibodies for evaluating LRRK2 signalling in cell biology and Parkinson's disease.

    Eyers, Patrick A

    The Biochemical journal

    2018  Band 475, Heft 1, Seite(n) 185–189

    Abstract: The addition of phosphate groups to substrates allows protein kinases to regulate a myriad of biological processes, and contextual analysis of protein-bound phosphate is important for understanding how kinases contribute to physiology and disease. ... ...

    Abstract The addition of phosphate groups to substrates allows protein kinases to regulate a myriad of biological processes, and contextual analysis of protein-bound phosphate is important for understanding how kinases contribute to physiology and disease. Leucine-rich repeat kinase 2 (LRRK2) is a Ser/Thr kinase linked to familial and sporadic cases of Parkinson's disease (PD). Recent work established that multiple Rab GTPases are physiological substrates of LRRK2, with Rab10 in particular emerging as a human substrate whose site-specific phosphorylation mirrors hyperactive LRRK2 lesions associated with PD. However, current assays to quantify Rab10 phosphorylation are expensive, time-consuming and technically challenging. In back-to-back studies reported in the
    Mesh-Begriff(e) Antibodies, Phospho-Specific ; Biological Phenomena ; Humans ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 ; Parkinson Disease ; Signal Transduction
    Chemische Substanzen Antibodies, Phospho-Specific ; LRRK2 protein, human (EC 2.7.11.1) ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1)
    Sprache Englisch
    Erscheinungsdatum 2018-01-05
    Erscheinungsland England
    Dokumenttyp Journal Article ; Comment
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20170870
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  4. Artikel ; Online: Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.

    Daly, Leonard A / Byrne, Dominic P / Perkins, Simon / Brownridge, Philip J / McDonnell, Euan / Jones, Andrew R / Eyers, Patrick A / Eyers, Claire E

    Journal of proteome research

    2023  Band 22, Heft 12, Seite(n) 3754–3772

    Abstract: Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalyzed by Golgi-resident tyrosyl protein sulfo transferases (TPSTs). Information on sY in humans is currently limited to ∼50 proteins, with only a handful having verified sites ...

    Abstract Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalyzed by Golgi-resident tyrosyl protein sulfo transferases (TPSTs). Information on sY in humans is currently limited to ∼50 proteins, with only a handful having verified sites of sulfation. As such, the contribution of sulfation to the regulation of biological processes remains poorly defined. Mass spectrometry (MS)-based proteomics is the method of choice for PTM analysis but has yet to be applied for systematic investigation of the "sulfome", primarily due to issues associated with discrimination of sY-containing from phosphotyrosine (pY)-containing peptides. In this study, we developed an MS-based workflow for sY-peptide characterization, incorporating optimized Zr
    Mesh-Begriff(e) Humans ; Phosphopeptides/analysis ; HEK293 Cells ; Workflow ; Tyrosine/metabolism ; Proteins ; Phosphotyrosine
    Chemische Substanzen Phosphopeptides ; tyrosine O-sulfate (29166358BF) ; Tyrosine (42HK56048U) ; Proteins ; Phosphotyrosine (21820-51-9)
    Sprache Englisch
    Erscheinungsdatum 2023-11-08
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.3c00425
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel: Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms.

    Bendzunas, George N / Byrne, Dominic P / Shrestha, Safal / Daly, Leonard A / Oswald, Sally O / Katiyar, Samiksha / Venkat, Aarya / Yeung, Wayland / Eyers, Claire E / Eyers, Patrick A / Kannan, Natarajan

    bioRxiv : the preprint server for biology

    2024  

    Abstract: In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs), including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment ... ...

    Abstract In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs), including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is known about how oxidation of cysteine residues modulate catalysis. In this study, we investigate redox regulation of the AMPK-related Brain-selective kinases (BRSK) 1 and 2, and detail how broad catalytic activity is directly regulated through reversible oxidation and reduction of evolutionarily conserved Cys residues within the catalytic domain. We show that redox-dependent control of BRSKs is a dynamic and multilayered process involving oxidative modifications of several Cys residues, including the formation of intramolecular disulfide bonds involving a pair of Cys residues near the catalytic HRD motif and a highly conserved T-Loop Cys with a BRSK-specific Cys within an unusual CPE motif at the end of the activation segment. Consistently, mutation of the CPE-Cys increases catalytic activity
    Sprache Englisch
    Erscheinungsdatum 2024-04-10
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.10.05.561145
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: 'Up with the LRRK': a phosphorylated Rab10 assay for evaluation of LRRK2 activity and inhibitor engagement.

    Eyers, Patrick A

    The Biochemical journal

    2016  Band 473, Heft 18, Seite(n) 2757–2762

    Abstract: Protein kinases catalyse the addition of phosphate groups to Ser/Thr and Tyr residues in cognate substrates and are mutated or hyperactive in a variety of diseases, making them important targets for rationally designed drugs. A good example is the ... ...

    Abstract Protein kinases catalyse the addition of phosphate groups to Ser/Thr and Tyr residues in cognate substrates and are mutated or hyperactive in a variety of diseases, making them important targets for rationally designed drugs. A good example is the Parkinson's disease-associated kinase, leucine-rich repeat kinase 2 (LRRK2), which is mutated (and probably hyperactive) in a small, but significant, subset of patients. An exciting new approach for personalised therapy is the development of central nervous system (CNS)-active small-molecule kinase inhibitors, which could be employed to 'normalise' LRRK2 signalling in affected cell types. However, the development of such drugs requires validated assays for the analysis of target engagement and the assembly of a set of tools for interrogating LRRK2, and its substrates, both in vitro and in vivo A new study published in the Biochemical Journal by Ito et al. establishes that a 'Phos-tag'™-binding assay can be exploited to measure phosphorylation of a recently identified LRRK2 substrate (Ras-related protein in brain 10 (Rab10)), and to compare and contrast relative catalytic output from disease-associated LRRK2 mutants. Powerful in vivo chemical genetic approaches are also disclosed, in which the catalytic activity of LRRK2 is unequivocally linked to the extent of Rab10 phosphorylation and the effects of chemically distinct LRRK2 inhibitors are matched with on-target inhibition mechanisms mediated through LRRK2 and its substrate Rab10. These important findings should simplify the generic analysis of Rab10 phosphorylation in model biological systems and are likely to be applicable to other substrates of LRRK2 (or indeed other kinases) for which phospho-specific antibodies are either absent or unsatisfactory.
    Mesh-Begriff(e) Humans ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/antagonists & inhibitors ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/metabolism ; Phosphorylation ; Protein Kinase Inhibitors/pharmacology ; Protein Transport ; rab GTP-Binding Proteins/metabolism
    Chemische Substanzen Protein Kinase Inhibitors ; LRRK2 protein, human (EC 2.7.11.1) ; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (EC 2.7.11.1) ; Rab10 protein, human (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Sprache Englisch
    Erscheinungsdatum 2016-09-26
    Erscheinungsland England
    Dokumenttyp Journal Article ; Comment
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20160671C
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  7. Artikel ; Online: Classification of Cushing's syndrome PKAc mutants based upon their ability to bind PKI.

    Omar, Mitchell H / Kihiu, Maryanne / Byrne, Dominic P / Lee, Kyung-Soon / Lakey, Tyler M / Butcher, Erik / Eyers, Patrick A / Scott, John D

    The Biochemical journal

    2024  Band 480, Heft 12, Seite(n) 875–890

    Abstract: Cushing's syndrome is an endocrine disorder caused by excess production of the stress hormone cortisol. Precision medicine strategies have identified single allele mutations within the PRKACA gene that drive adrenal Cushing's syndrome. These mutations ... ...

    Abstract Cushing's syndrome is an endocrine disorder caused by excess production of the stress hormone cortisol. Precision medicine strategies have identified single allele mutations within the PRKACA gene that drive adrenal Cushing's syndrome. These mutations promote perturbations in the catalytic core of protein kinase A (PKAc) that impair autoinhibition by regulatory subunits and compartmentalization via recruitment into AKAP signaling islands. PKAcL205R is found in ∼45% of patients, whereas PKAcE31V, PKAcW196R, and L198insW and C199insV insertion mutants are less prevalent. Mass spectrometry, cellular, and biochemical data indicate that Cushing's PKAc variants fall into two categories: those that interact with the heat-stable protein kinase inhibitor PKI, and those that do not. In vitro activity measurements show that wild-type PKAc and W196R activities are strongly inhibited by PKI (IC50 < 1 nM). In contrast, PKAcL205R activity is not blocked by the inhibitor. Immunofluorescent analyses show that the PKI-binding variants wild-type PKAc, E31V, and W196R are excluded from the nucleus and protected against proteolytic processing. Thermal stability measurements reveal that upon co-incubation with PKI and metal-bound nucleotide, the W196R variant tolerates melting temperatures 10°C higher than PKAcL205. Structural modeling maps PKI-interfering mutations to a ∼20 Å diameter area at the active site of the catalytic domain that interfaces with the pseudosubstrate of PKI. Thus, Cushing's kinases are individually controlled, compartmentalized, and processed through their differential association with PKI.
    Mesh-Begriff(e) Humans ; Cushing Syndrome/genetics ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Mutation ; Catalytic Domain
    Chemische Substanzen Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
    Sprache Englisch
    Erscheinungsdatum 2024-05-30
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20230183
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  8. Artikel ; Online: Analysis of human Tribbles 2 (TRIB2) pseudokinase.

    Harris, John A / Fairweather, Emma / Byrne, Dominic P / Eyers, Patrick A

    Methods in enzymology

    2022  Band 667, Seite(n) 79–99

    Abstract: Human Tribbles 2 (TRIB2) is a cancer-associated pseudokinase with a broad human protein interactome, including the well-studied AKT, C/EBPα and MAPK modules. Several lines of evidence indicate that human TRIB2 promotes cell survival and drug-resistance ... ...

    Abstract Human Tribbles 2 (TRIB2) is a cancer-associated pseudokinase with a broad human protein interactome, including the well-studied AKT, C/EBPα and MAPK modules. Several lines of evidence indicate that human TRIB2 promotes cell survival and drug-resistance in solid tumors and blood cancers and is therefore of interest as a potential therapeutic target, although its physiological functions remain relatively poorly understood. The unique TRIB2 pseudokinase domain lacks the canonical 'DFG' motif, and subsequently possesses very low affinity for ATP in both the presence and absence of metal ions. However, TRIB2 also contains a unique cysteine-rich αC-helix, which interacts with a conserved peptide motif in its own carboxyl-terminal tail. This regulatory flanking region drives regulated interactions with distinct E3 ubiquitin ligases that serve to control the stability and turnover of TRIB2 client proteins. TRIB2 is also a low-affinity target of several known small-molecule protein kinase inhibitors, which were originally identified using purified recombinant TRIB2 proteins and a thermal shift assay. In this chapter, we discuss laboratory-based procedures for purification, stabilization and analysis of human TRIB2, including screening procedures that can be used for the identification of both reversible and covalent small molecule ligands.
    Mesh-Begriff(e) Calcium-Calmodulin-Dependent Protein Kinases/genetics ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Neoplasms/pathology ; Ubiquitin-Protein Ligases/metabolism
    Chemische Substanzen Intracellular Signaling Peptides and Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; TRIB2 protein, human (EC 2.7.11.17)
    Sprache Englisch
    Erscheinungsdatum 2022-04-13
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2022.03.025
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel ; Online: TRIBBLES: A Twist in the Pseudokinase Tail.

    Eyers, Patrick A

    Structure (London, England : 1993)

    2015  Band 23, Heft 11, Seite(n) 1974–1976

    Abstract: TRIB1, a homolog of Drosophila Tribbles, regulates the stability of transcription factors through physical interaction with the ubiquitin E3 ligase COP1. In this issue of Structure, Murphy et al. (2015) report the first X-ray analysis of the TRIB1 ... ...

    Abstract TRIB1, a homolog of Drosophila Tribbles, regulates the stability of transcription factors through physical interaction with the ubiquitin E3 ligase COP1. In this issue of Structure, Murphy et al. (2015) report the first X-ray analysis of the TRIB1 pseudokinase domain and its C-terminal COP1-binding extension.
    Mesh-Begriff(e) Animals ; Intracellular Signaling Peptides and Proteins ; Models, Molecular ; Protein Binding ; Transcription Factors/chemistry ; Ubiquitin-Protein Ligases/metabolism
    Chemische Substanzen Intracellular Signaling Peptides and Proteins ; Transcription Factors ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Sprache Englisch
    Erscheinungsdatum 2015-11-03
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Comment
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2015.10.003
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  10. Artikel ; Online: Discovery of a Cushing's syndrome protein kinase A mutant that biases signaling through type I AKAPs.

    Omar, Mitchell H / Byrne, Dominic P / Shrestha, Safal / Lakey, Tyler M / Lee, Kyung-Soon / Lauer, Sophia M / Collins, Kerrie B / Daly, Leonard A / Eyers, Claire E / Baird, Geoffrey S / Ong, Shao-En / Kannan, Natarajan / Eyers, Patrick A / Scott, John D

    Science advances

    2024  Band 10, Heft 8, Seite(n) eadl1258

    Abstract: Adrenal Cushing's syndrome is a disease of cortisol hypersecretion often caused by mutations in protein kinase A catalytic subunit (PKAc). Using a personalized medicine screening platform, we discovered a Cushing's driver mutation, PKAc-W196G, in ~20% of ...

    Abstract Adrenal Cushing's syndrome is a disease of cortisol hypersecretion often caused by mutations in protein kinase A catalytic subunit (PKAc). Using a personalized medicine screening platform, we discovered a Cushing's driver mutation, PKAc-W196G, in ~20% of patient samples analyzed. Proximity proteomics and photokinetic imaging reveal that PKAc
    Mesh-Begriff(e) Humans ; Cushing Syndrome/genetics ; A Kinase Anchor Proteins/genetics ; A Kinase Anchor Proteins/metabolism ; Signal Transduction ; Catalytic Domain ; Bias
    Chemische Substanzen A Kinase Anchor Proteins
    Sprache Englisch
    Erscheinungsdatum 2024-02-21
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.adl1258
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