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Articles by Daniel Horn-Ghetko
Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex - Nature Structural & Molecular Biology
Abstract Ubiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such domains, ‘cullin–RING’ and ‘RBR’, are individually found in several hundred human E3 ligases, and collaborate with E2 enzymes to catalyze ubiquitylation. However, the vertebrate-specific CUL9 complex with RBX1 (also called ROC1), of interest due to its tumor suppressive interaction with TP53, uniquely encompasses both cullin–RING and RBR domains.
Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5 - Nature Chemical Biology
Abstract Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry and cryo‐electron microscopy (cryo‐EM) to visualize stable mimics of the intermediates along K48-linked Ub chain formation by the human E3, UBR5.
Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5
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A Pro‐Fluorescent Ubiquitin‐Based Probe to Monitor Cysteine‐Based E3 Ligase Activity
A Powerful Platform for HTS Having validated the reactivity and high sensitivity of the UbSRhodol reagent in real time, we set out to test UbSRhodol for High-Throughput Screening (HTS) campaigns. As a proof of concept, we employed a fragment-based ligand discovery approach to identify transthiolation blockers for three E3 ligases, namely the homologous RBR E3 ligases HOIP and ARIH1OPEN and the HECT E3 ligase SMURF1, to investigate if a different subset of unique hits could be retrieved.
Ubiquitin ligation to F-box protein targets by SCF-RBR E3-E3 super-assembly
Abstract 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-assemblies3,4,5,6,7.
Proximity-triggered covalent stabilization of low-affinity protein complexes in vitro and in vivo
The characterization of low-affinity protein complexes is challenging due to their dynamic nature. Here we present a method to stabilize transient protein complexes in vivo by generating a covalent and conformationally flexible bridge between the interaction partners. A highly active pyrrolysyl tRNA synthetase mutant directs the incorporation of unnatural amino acids bearing bromoalkyl moieties (BrCnK) into proteins.
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