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Keywords {🔍}

arih, ubiquitin, substrate, pubmed, domain, neddylated, data, article, fig, google, scholar, catalytic, cyclin, scf, cas, ubel, ubiquitylation, extended, reaction, substrates, abp, fbox, cysteine, ligase, protein, structure, central, transfer, complex, nature, helix, nedd, cul, rcat, cryoem, ubed, ligases, map, proteins, structures, peptide, bound, terminus, mechanism, ring, rbx, eeact, cell, ariadne, phosphopeptide,

Topics {✒️}

low-pass-filtered cryo-em maps low-pass-filtered cryo-em map nature portfolio neddylated cul1–rbx1–skp1–skp2–ckshs1–p27–cyclin privacy policy e1–e2–e3 tri-enzyme cascades scf–rbr e3–e3 super-assembly humans—form e3–e3 super-assemblies3 neddylated cul1–rbx1-activated arih1~ubiquitin~substrate 3-dioxolan-2-yl]prop-2-en-1-amine f-box-protein-bound substrate proceeds arih1–nedd8–cul1–rbx1–skp1–skp2–ckshs1 skp1–f-box-protein substrate receptor versatile e3–e3 super-assembly skp1–skp2–ckshs1–phospho-p27–cyclin advertising e3–e3act super-domain adjoins e3–e3act super-domain appears abundant ‘e3–e3act super-domain phospho-ubiquitin-induced parkin activation treatment withtrifluoroacetic acid/triisopropylsilane/water high-resolution cryo-em data e3–e3-catalysed substrate ubiquitylation adjacent e3–e3act super-domain f-box protein–substrate assembly cul1-whb-domain-linked nedd8 interactions social media e3–e3act super-domain contributing interchangeable substrate-specific receptor e2-type ubiquitin-carrying enzymes arih1–nedd8–cul1–rbx1–skp1–fbxw7 f-box protein β-trcp f-box-protein-bound substrate cul1–rbx1–skp1–skp2-ckshs1 ckshs1–skp2–skp1–cul1–rbx1 e3–e3 post-ts1 intermediate neddylated scf–arih1-catalysed ubiquitylation high-resolution cryo-em structures f-box-protein-binding degron ice‐cold pentane/diethyl ether specific f-box protein research design exploratory research research hospital phosphopepeptide-bound substrate-binding domain f-box protein targets cul5-mediated apobec3g degradation caenorhabditis elegans development cdc53p/cullin catalyzes ubiquitination reprints

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         headline:Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly
         description:E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates1,2. However, rather than functioning individually, many neddylated cullin–RING E3 ligases (CRLs) and RBR-type E3 ligases in the ARIH family—which together account for nearly half of all ubiquitin ligases in humans—form E3–E3 super-assemblies3–7. Here, by studying CRLs in the SKP1–CUL1–F-box (SCF) family, we show how neddylated SCF ligases and ARIH1 (an RBR-type E3 ligase) co-evolved to ubiquitylate diverse substrates presented on various F-box proteins. We developed activity-based chemical probes that enabled cryo-electron microscopy visualization of steps in E3–E3 ubiquitylation, initiating with ubiquitin linked to the E2 enzyme UBE2L3, then transferred to the catalytic cysteine of ARIH1, and culminating in ubiquitin linkage to a substrate bound to the SCF E3 ligase. The E3–E3 mechanism places the ubiquitin-linked active site of ARIH1 adjacent to substrates bound to F-box proteins (for example, substrates with folded structures or limited length) that are incompatible with previously described conventional RING E3-only mechanisms. The versatile E3–E3 super-assembly may therefore underlie widespread ubiquitylation. Cryo-electron microscopy of neddylated SCF-family ligases interacting with the RBR-type E3 ligase ARIH1 reveals the steps through which E3–E3 super-assemblies ubiquitylate a diverse set of substrates presented on F-box proteins.
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      headline:Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly
      description:E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates1,2. However, rather than functioning individually, many neddylated cullin–RING E3 ligases (CRLs) and RBR-type E3 ligases in the ARIH family—which together account for nearly half of all ubiquitin ligases in humans—form E3–E3 super-assemblies3–7. Here, by studying CRLs in the SKP1–CUL1–F-box (SCF) family, we show how neddylated SCF ligases and ARIH1 (an RBR-type E3 ligase) co-evolved to ubiquitylate diverse substrates presented on various F-box proteins. We developed activity-based chemical probes that enabled cryo-electron microscopy visualization of steps in E3–E3 ubiquitylation, initiating with ubiquitin linked to the E2 enzyme UBE2L3, then transferred to the catalytic cysteine of ARIH1, and culminating in ubiquitin linkage to a substrate bound to the SCF E3 ligase. The E3–E3 mechanism places the ubiquitin-linked active site of ARIH1 adjacent to substrates bound to F-box proteins (for example, substrates with folded structures or limited length) that are incompatible with previously described conventional RING E3-only mechanisms. The versatile E3–E3 super-assembly may therefore underlie widespread ubiquitylation. Cryo-electron microscopy of neddylated SCF-family ligases interacting with the RBR-type E3 ligase ARIH1 reveals the steps through which E3–E3 super-assemblies ubiquitylate a diverse set of substrates presented on F-box proteins.
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         Ubiquitylated proteins
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      name:Oncode Institute, Department of Cell and Chemical Biology, Chemical Immunology, Leiden University Medical Centre, Leiden, The Netherlands
      name:Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany
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      name:Oncode Institute, Department of Cell and Chemical Biology, Chemical Immunology, Leiden University Medical Centre, Leiden, The Netherlands
      name:Department of Chemistry and Biochemistry, University of Nevada, Las Vegas, Las Vegas, USA
      name:Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany
      name:Department of Structural Biology, St Jude Children’s Research Hospital, Memphis, USA

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