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Keywords {🔍}

striatin, mst, ppa, binding, domain, figure, mob, wildtype, pubmed, coiledcoil, residues, complexes, mutants, mutant, article, cells, protein, google, scholar, phosphorylation, cas, cell, family, subunit, association, proteins, results, deletion, oligomerization, activation, threonine, striatins, sgna, phosphatase, bind, acid, ccm, striatinassociated, central, okadaic, experiments, lysates, antibody, kinase, caveolinbinding, calmodulinbinding, relative, gel, binds, autophosphorylation,

Topics {✒️}

modified plenti6/v5-d-topo plasmid plasmid plenti6/v5-d-topo f7 anti-ha-agarose conjugate make pegfp-n3-wild-type striatin flag epitope-tagged wild-type 84a/94a/105a mutant effects plenti6/v5-d-topo fluor s-max chemilumimager ha-tagged r100s/r101e striatin m2 anti-flag antibody ha-tagged wild-type striatin pegfp-n3-wild-type striatin open access article requires n-terminal sequences protein-tyrosine phosphatase-pest article download pdf immunoprecipitate ha-tagged proteins striatin mutant l84a/l94a/l105a ha-tagged wild-type anti-ha antibody 16b12 genome-wide association identifies flag epitope-tag immunoprecipitates germinal center kinase-iii multi-domain scaffolding protein c-terminal truncation mutants coiled-coil oligomerization-state specificity exogenously expressed wild-type phospho-specific antibody recognizing xbai-apai digested backbone multiple protein-binding domains transfected ha-tagged striatins flag-tagged mst3 isoform 12ca5 anti-ha antibody flag-tagged mst3 proteins n-terminal deletion mutant c-terminal deletion mutants striatin sequences c-terminal c-terminal striatin sequences gc-rich striatin sequences protein phosphatase 2a modified lentivirus plasmid cyclin-dependent protein kinases wild-type striatin expressed wd-repeat protein present calmodulin-dependent scaffolding protein weighted n-terminal ends t182a mst3-expressing cells ha-epitope tag gfp expressing plasmid mutant l84a/l94a/i102a

Schema {🗺️}

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         headline:Protein phosphatase 2a (PP2A) binds within the oligomerization domain of striatin and regulates the phosphorylation and activation of the mammalian Ste20-Like kinase Mst3
         description:Striatin, a putative protein phosphatase 2A (PP2A) B-type regulatory subunit, is a multi-domain scaffolding protein that has recently been linked to several diseases including cerebral cavernous malformation (CCM), which causes symptoms ranging from headaches to stroke. Striatin association with the PP2A A/C (structural subunit/catalytic subunit) heterodimer alters PP2A substrate specificity, but targets and roles of striatin-associated PP2A are not known. In addition to binding the PP2A A/C heterodimer to form a PP2A holoenzyme, striatin associates with cerebral cavernous malformation 3 (CCM3) protein, the mammalian Mps one binder (MOB) homolog, Mob3/phocein, the mammalian sterile 20-like (Mst) kinases, Mst3, Mst4 and STK25, and several other proteins to form a large signaling complex. Little is known about the molecular architecture of the striatin complex and the regulation of these sterile 20-like kinases. To help define the molecular organization of striatin complexes and to determine whether Mst3 might be negatively regulated by striatin-associated PP2A, a structure-function analysis of striatin was performed. Two distinct regions of striatin are capable of stably binding directly or indirectly to Mob3--one N-terminal, including the coiled-coil domain, and another more C-terminal, including the WD-repeat domain. In addition, striatin residues 191-344 contain determinants necessary for efficient association of Mst3, Mst4, and CCM3. PP2A associates with the coiled-coil domain of striatin, but unlike Mob3 and Mst3, its binding appears to require striatin oligomerization. Deletion of the caveolin-binding domain on striatin abolishes striatin family oligomerization and PP2A binding. Point mutations in striatin that disrupt PP2A association cause hyperphosphorylation and activation of striatin-associated Mst3. Striatin orchestrates the regulation of Mst3 by PP2A. It binds Mst3 likely as a dimer with CCM3 via residues lying between striatin's calmodulin-binding and WD-domains and recruits the PP2A A/C heterodimer to its coiled-coil/oligomerization domain. Residues outside the previously reported coiled-coil domain of striatin are necessary for its oligomerization. Striatin-associated PP2A is critical for Mst3 dephosphorylation and inactivation. Upon inhibition of PP2A, Mst3 activation appears to involve autophosphorylation of multiple activation loop phosphorylation sites. Mob3 can associate with striatin sequences C-terminal to the Mst3 binding site but also with sequences proximal to striatin-associated PP2A, consistent with a possible role for Mob 3 in the regulation of Mst3 by PP2A.
         datePublished:2011-10-10T00:00:00Z
         dateModified:2011-10-10T00:00:00Z
         pageStart:1
         pageEnd:18
         license:https://creativecommons.org/licenses/by/2.0
         sameAs:https://doi.org/10.1186/1471-2091-12-54
         keywords:
            Okadaic Acid
            Vesicular Trafficking
            Mob3 Binding
            PP2A Holoenzyme
            Mst4 Kinase
            Biochemistry
            general
            Life Sciences
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      headline:Protein phosphatase 2a (PP2A) binds within the oligomerization domain of striatin and regulates the phosphorylation and activation of the mammalian Ste20-Like kinase Mst3
      description:Striatin, a putative protein phosphatase 2A (PP2A) B-type regulatory subunit, is a multi-domain scaffolding protein that has recently been linked to several diseases including cerebral cavernous malformation (CCM), which causes symptoms ranging from headaches to stroke. Striatin association with the PP2A A/C (structural subunit/catalytic subunit) heterodimer alters PP2A substrate specificity, but targets and roles of striatin-associated PP2A are not known. In addition to binding the PP2A A/C heterodimer to form a PP2A holoenzyme, striatin associates with cerebral cavernous malformation 3 (CCM3) protein, the mammalian Mps one binder (MOB) homolog, Mob3/phocein, the mammalian sterile 20-like (Mst) kinases, Mst3, Mst4 and STK25, and several other proteins to form a large signaling complex. Little is known about the molecular architecture of the striatin complex and the regulation of these sterile 20-like kinases. To help define the molecular organization of striatin complexes and to determine whether Mst3 might be negatively regulated by striatin-associated PP2A, a structure-function analysis of striatin was performed. Two distinct regions of striatin are capable of stably binding directly or indirectly to Mob3--one N-terminal, including the coiled-coil domain, and another more C-terminal, including the WD-repeat domain. In addition, striatin residues 191-344 contain determinants necessary for efficient association of Mst3, Mst4, and CCM3. PP2A associates with the coiled-coil domain of striatin, but unlike Mob3 and Mst3, its binding appears to require striatin oligomerization. Deletion of the caveolin-binding domain on striatin abolishes striatin family oligomerization and PP2A binding. Point mutations in striatin that disrupt PP2A association cause hyperphosphorylation and activation of striatin-associated Mst3. Striatin orchestrates the regulation of Mst3 by PP2A. It binds Mst3 likely as a dimer with CCM3 via residues lying between striatin's calmodulin-binding and WD-domains and recruits the PP2A A/C heterodimer to its coiled-coil/oligomerization domain. Residues outside the previously reported coiled-coil domain of striatin are necessary for its oligomerization. Striatin-associated PP2A is critical for Mst3 dephosphorylation and inactivation. Upon inhibition of PP2A, Mst3 activation appears to involve autophosphorylation of multiple activation loop phosphorylation sites. Mob3 can associate with striatin sequences C-terminal to the Mst3 binding site but also with sequences proximal to striatin-associated PP2A, consistent with a possible role for Mob 3 in the regulation of Mst3 by PP2A.
      datePublished:2011-10-10T00:00:00Z
      dateModified:2011-10-10T00:00:00Z
      pageStart:1
      pageEnd:18
      license:https://creativecommons.org/licenses/by/2.0
      sameAs:https://doi.org/10.1186/1471-2091-12-54
      keywords:
         Okadaic Acid
         Vesicular Trafficking
         Mob3 Binding
         PP2A Holoenzyme
         Mst4 Kinase
         Biochemistry
         general
         Life Sciences
      image:
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                     type:PostalAddress
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            name:Emory University School of Medicine
            address:
               name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:Emory University School of Medicine
            address:
               name:Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
      name:Karma J Carrier
      affiliation:
            name:Emory University School of Medicine
            address:
               name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:Meso Scale Discovery
            address:
               name:Meso Scale Discovery, Gaithersburg, USA
               type:PostalAddress
            type:Organization
      name:Candace A Jones
      affiliation:
            name:Emory University School of Medicine
            address:
               name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:Emory University School of Medicine
            address:
               name:Postdoctoral Fellowships in Research & Science Teaching (FIRST) Program, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:North Louisiana Criminalistics Laboratory
            address:
               name:North Louisiana Criminalistics Laboratory, Shreveport, USA
               type:PostalAddress
            type:Organization
      name:Quiana L Kern
      affiliation:
            name:Emory University School of Medicine
            address:
               name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:Emory University School of Medicine
            address:
               name:Department of Anesthesiology, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
      name:Carlos S Moreno
      affiliation:
            name:Emory University School of Medicine
            address:
               name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:Emory University School of Medicine
            address:
               name:Department of Pathology and Laboratory of Medicine, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
      name:Richard H Karas
      affiliation:
            name:Molecular Cardiology Research Institute, Tufts Medical Center
            address:
               name:Department of Medicine, Molecular Cardiology Research Institute, Tufts Medical Center, Boston, USA
               type:PostalAddress
            type:Organization
      name:David C Pallas
      affiliation:
            name:Emory University School of Medicine
            address:
               name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:Emory University School of Medicine
            address:
               name:Postdoctoral Fellowships in Research & Science Teaching (FIRST) Program, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
            name:Emory University School of Medicine
            address:
               name:Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, Atlanta, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
      name:Postdoctoral Fellowships in Research & Science Teaching (FIRST) Program, Emory University School of Medicine, Atlanta, USA
      name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
      name:Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, Atlanta, USA
      name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
      name:Meso Scale Discovery, Gaithersburg, USA
      name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
      name:Postdoctoral Fellowships in Research & Science Teaching (FIRST) Program, Emory University School of Medicine, Atlanta, USA
      name:North Louisiana Criminalistics Laboratory, Shreveport, USA
      name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
      name:Department of Anesthesiology, Emory University School of Medicine, Atlanta, USA
      name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
      name:Department of Pathology and Laboratory of Medicine, Emory University School of Medicine, Atlanta, USA
      name:Department of Medicine, Molecular Cardiology Research Institute, Tufts Medical Center, Boston, USA
      name:Department of Biochemistry and Winship Cancer Institute, Emory University School of Medicine, Atlanta, USA
      name:Postdoctoral Fellowships in Research & Science Teaching (FIRST) Program, Emory University School of Medicine, Atlanta, USA
      name:Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, Atlanta, USA

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• Google Tag Manager

Libraries {📚}

• Clipboard.js
• Prism.js

CDN Services {📦}

• Crossref
• Pbgrd