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  1. Article ; Online: Identification of a SARS-like bat coronavirus that shares structural features with the spike glycoprotein receptor-binding domain of SARS-CoV-2.

    Fraguas Bringas, Conchita / Booth, David

    Access microbiology

    2020  Volume 2, Issue 11, Page(s) acmi000166

    Abstract: SARS-CoV-2 is a recently emerged coronavirus that binds angiotensin-converting enzyme 2 (ACE2) for cell entry via its receptor-binding domain (RBD) on a surface-expressed spike glycoprotein. Studies show that despite its similarities to severe acute ... ...

    Abstract SARS-CoV-2 is a recently emerged coronavirus that binds angiotensin-converting enzyme 2 (ACE2) for cell entry via its receptor-binding domain (RBD) on a surface-expressed spike glycoprotein. Studies show that despite its similarities to severe acute respiratory syndrome (SARS) coronavirus, there are critical differences in key RBD residues when compared to SARS-CoV-2. Here we present a short
    Language English
    Publishing date 2020-09-08
    Publishing country England
    Document type Journal Article
    ISSN 2516-8290
    ISSN (online) 2516-8290
    DOI 10.1099/acmi.0.000166
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: CaMKK2 is not involved in contraction-stimulated AMPK activation and glucose uptake in skeletal muscle.

    Negoita, Florentina / Addinsall, Alex B / Hellberg, Kristina / Bringas, Conchita Fraguas / Hafen, Paul S / Sermersheim, Tyler J / Agerholm, Marianne / Lewis, Christopher T A / Ahwazi, Danial / Ling, Naomi X Y / Larsen, Jeppe K / Deshmukh, Atul S / Hossain, Mohammad A / Oakhill, Jonathan S / Ochala, Julien / Brault, Jeffrey J / Sankar, Uma / Drewry, David H / Scott, John W /
    Witczak, Carol A / Sakamoto, Kei

    Molecular metabolism

    2023  Volume 75, Page(s) 101761

    Abstract: Objective: The AMP-activated protein kinase (AMPK) gets activated in response to energetic stress such as contractions and plays a vital role in regulating various metabolic processes such as insulin-independent glucose uptake in skeletal muscle. The ... ...

    Abstract Objective: The AMP-activated protein kinase (AMPK) gets activated in response to energetic stress such as contractions and plays a vital role in regulating various metabolic processes such as insulin-independent glucose uptake in skeletal muscle. The main upstream kinase that activates AMPK through phosphorylation of α-AMPK Thr172 in skeletal muscle is LKB1, however some studies have suggested that Ca
    Methods: A recently developed CaMKK2 inhibitor (SGC-CAMKK2-1) alongside a structurally related but inactive compound (SGC-CAMKK2-1N), as well as CaMKK2 knock-out (KO) mice were used. In vitro kinase inhibition selectivity and efficacy assays, as well as cellular inhibition efficacy analyses of CaMKK inhibitors (STO-609 and SGC-CAMKK2-1) were performed. Phosphorylation and activity of AMPK following contractions (ex vivo) in mouse skeletal muscles treated with/without CaMKK inhibitors or isolated from wild-type (WT)/CaMKK2 KO mice were assessed. Camkk2 mRNA in mouse tissues was measured by qPCR. CaMKK2 protein expression was assessed by immunoblotting with or without prior enrichment of calmodulin-binding proteins from skeletal muscle extracts, as well as by mass spectrometry-based proteomics of mouse skeletal muscle and C2C12 myotubes.
    Results: STO-609 and SGC-CAMKK2-1 were equally potent and effective in inhibiting CaMKK2 in cell-free and cell-based assays, but SGC-CAMKK2-1 was much more selective. Contraction-stimulated phosphorylation and activation of AMPK were not affected with CaMKK inhibitors or in CaMKK2 null muscles. Contraction-stimulated glucose uptake was comparable between WT and CaMKK2 KO muscle. Both CaMKK inhibitors (STO-609 and SGC-CAMKK2-1) and the inactive compound (SGC-CAMKK2-1N) significantly inhibited contraction-stimulated glucose uptake. SGC-CAMKK2-1 also inhibited glucose uptake induced by a pharmacological AMPK activator or insulin. Relatively low levels of Camkk2 mRNA were detected in mouse skeletal muscle, but neither CaMKK2 protein nor its derived peptides were detectable in mouse skeletal muscle tissue.
    Conclusions: We demonstrate that pharmacological inhibition or genetic loss of CaMKK2 does not affect contraction-stimulated AMPK phosphorylation and activation, as well as glucose uptake in skeletal muscle. Previously observed inhibitory effect of STO-609 on AMPK activity and glucose uptake is likely due to off-target effects. CaMKK2 protein is either absent from adult murine skeletal muscle or below the detection limit of currently available methods.
    MeSH term(s) Animals ; Mice ; AMP-Activated Protein Kinases/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Kinase/metabolism ; Glucose/metabolism ; Insulins/metabolism ; Mice, Knockout ; Muscle, Skeletal/metabolism ; Protein Serine-Threonine Kinases/metabolism
    Chemical Substances AMP-Activated Protein Kinases (EC 2.7.11.31) ; Calcium-Calmodulin-Dependent Protein Kinase Kinase (EC 2.7.11.17) ; Glucose (IY9XDZ35W2) ; Insulins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; STO 609 ; Camkk2 protein, mouse (EC 2.7.11.17)
    Language English
    Publishing date 2023-06-26
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2708735-9
    ISSN 2212-8778 ; 2212-8778
    ISSN (online) 2212-8778
    ISSN 2212-8778
    DOI 10.1016/j.molmet.2023.101761
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: BUB-1 targets PP2A:B56 to regulate chromosome congression during meiosis I in

    Bel Borja, Laura / Soubigou, Flavie / Taylor, Samuel J P / Fraguas Bringas, Conchita / Budrewicz, Jacqueline / Lara-Gonzalez, Pablo / Sorensen Turpin, Christopher G / Bembenek, Joshua N / Cheerambathur, Dhanya K / Pelisch, Federico

    eLife

    2020  Volume 9

    Abstract: Protein Phosphatase 2A (PP2A) is a heterotrimer composed of scaffolding (A), catalytic (C), and regulatory (B) subunits. PP2A complexes with B56 subunits are targeted by Shugoshin and BUBR1 to protect centromeric cohesion and stabilise kinetochore- ... ...

    Abstract Protein Phosphatase 2A (PP2A) is a heterotrimer composed of scaffolding (A), catalytic (C), and regulatory (B) subunits. PP2A complexes with B56 subunits are targeted by Shugoshin and BUBR1 to protect centromeric cohesion and stabilise kinetochore-microtubule attachments in yeast and mouse meiosis. In
    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/metabolism ; Caenorhabditis elegans Proteins/physiology ; Chromosome Segregation ; Chromosomes/physiology ; Meiosis/physiology ; Oocytes/metabolism ; Oocytes/physiology ; Protein Phosphatase 2/metabolism ; Protein Phosphatase 2/physiology ; Protein Serine-Threonine Kinases/metabolism ; Protein Serine-Threonine Kinases/physiology
    Chemical Substances Caenorhabditis elegans Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; bub-1 protein, C elegans (EC 2.7.11.1) ; Protein Phosphatase 2 (EC 3.1.3.16)
    Language English
    Publishing date 2020-12-23
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.65307
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: BUB-1 targets PP2A:B56 to regulate chromosome congression during meiosis I in C. elegans oocytes

    Laura Bel Borja / Flavie Soubigou / Samuel J P Taylor / Conchita Fraguas Bringas / Jacqueline Budrewicz / Pablo Lara-Gonzalez / Christopher G Sorensen Turpin / Joshua N Bembenek / Dhanya K Cheerambathur / Federico Pelisch

    eLife, Vol

    2020  Volume 9

    Abstract: Protein Phosphatase 2A (PP2A) is a heterotrimer composed of scaffolding (A), catalytic (C), and regulatory (B) subunits. PP2A complexes with B56 subunits are targeted by Shugoshin and BUBR1 to protect centromeric cohesion and stabilise kinetochore– ... ...

    Abstract Protein Phosphatase 2A (PP2A) is a heterotrimer composed of scaffolding (A), catalytic (C), and regulatory (B) subunits. PP2A complexes with B56 subunits are targeted by Shugoshin and BUBR1 to protect centromeric cohesion and stabilise kinetochore–microtubule attachments in yeast and mouse meiosis. In Caenorhabditis elegans, the closest BUBR1 orthologue lacks the B56-interaction domain and Shugoshin is not required for meiotic segregation. Therefore, the role of PP2A in C. elegans female meiosis is unknown. We report that PP2A is essential for meiotic spindle assembly and chromosome dynamics during C. elegans female meiosis. BUB-1 is the main chromosome-targeting factor for B56 subunits during prometaphase I. BUB-1 recruits PP2A:B56 to the chromosomes via a newly identified LxxIxE motif in a phosphorylation-dependent manner, and this recruitment is important for proper chromosome congression. Our results highlight a novel mechanism for B56 recruitment, essential for recruiting a pool of PP2A involved in chromosome congression during meiosis I.
    Keywords PP2A ; meiosis ; Bub1 ; B56 ; SLiM ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2020-12-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: CaMKK2 is not involved in contraction-stimulated AMPK activation and glucose uptake in skeletal muscle

    Florentina Negoita / Alex B. Addinsall / Kristina Hellberg / Conchita Fraguas Bringas / Paul S. Hafen / Tyler J. Sermersheim / Marianne Agerholm / Christopher T.A. Lewis / Danial Ahwazi / Naomi X.Y. Ling / Jeppe K. Larsen / Atul S. Deshmukh / Mohammad A. Hossain / Jonathan S. Oakhill / Julien Ochala / Jeffrey J. Brault / Uma Sankar / David H. Drewry / John W. Scott /
    Carol A. Witczak / Kei Sakamoto

    Molecular Metabolism, Vol 75, Iss , Pp 101761- (2023)

    2023  

    Abstract: Objective: The AMP-activated protein kinase (AMPK) gets activated in response to energetic stress such as contractions and plays a vital role in regulating various metabolic processes such as insulin-independent glucose uptake in skeletal muscle. The ... ...

    Abstract Objective: The AMP-activated protein kinase (AMPK) gets activated in response to energetic stress such as contractions and plays a vital role in regulating various metabolic processes such as insulin-independent glucose uptake in skeletal muscle. The main upstream kinase that activates AMPK through phosphorylation of α-AMPK Thr172 in skeletal muscle is LKB1, however some studies have suggested that Ca2+/calmodulin-dependent protein kinase kinase 2 (CaMKK2) acts as an alternative kinase to activate AMPK. We aimed to establish whether CaMKK2 is involved in activation of AMPK and promotion of glucose uptake following contractions in skeletal muscle. Methods: A recently developed CaMKK2 inhibitor (SGC-CAMKK2-1) alongside a structurally related but inactive compound (SGC-CAMKK2-1N), as well as CaMKK2 knock-out (KO) mice were used. In vitro kinase inhibition selectivity and efficacy assays, as well as cellular inhibition efficacy analyses of CaMKK inhibitors (STO-609 and SGC-CAMKK2-1) were performed. Phosphorylation and activity of AMPK following contractions (ex vivo) in mouse skeletal muscles treated with/without CaMKK inhibitors or isolated from wild-type (WT)/CaMKK2 KO mice were assessed. Camkk2 mRNA in mouse tissues was measured by qPCR. CaMKK2 protein expression was assessed by immunoblotting with or without prior enrichment of calmodulin-binding proteins from skeletal muscle extracts, as well as by mass spectrometry-based proteomics of mouse skeletal muscle and C2C12 myotubes. Results: STO-609 and SGC-CAMKK2-1 were equally potent and effective in inhibiting CaMKK2 in cell-free and cell-based assays, but SGC-CAMKK2-1 was much more selective. Contraction-stimulated phosphorylation and activation of AMPK were not affected with CaMKK inhibitors or in CaMKK2 null muscles. Contraction-stimulated glucose uptake was comparable between WT and CaMKK2 KO muscle. Both CaMKK inhibitors (STO-609 and SGC-CAMKK2-1) and the inactive compound (SGC-CAMKK2-1N) significantly inhibited contraction-stimulated glucose uptake. ...
    Keywords Ca2+/calmodulin dependent protein kinase kinase 2 ; AMP-activated protein kinase ; SGC-CAMKK2-1 ; STO-609 ; Glucose uptake ; Internal medicine ; RC31-1245
    Language English
    Publishing date 2023-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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