Ubiquitin in Motion: Structural Studies of the Ubiquitin-Conjugating Enzyme∼Ubiquitin Conjugate [PDF]
Biochemistry, 2011 Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer
Jonathan N, Pruneda +4 more
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NEDD8-conjugating enzyme E2s: critical targets for cancer therapy
Cell Death Discovery, 2023 NEDD8-conjugating enzymes, E2s, include the well-studied ubiquitin-conjugating enzyme E2 M (UBE2M) and the poorly characterized ubiquitin-conjugating enzyme E2 F (UBE2F).
Lisha Zhou +7 more
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Solution Structure of the Ubiquitin-conjugating Enzyme UbcH5B [PDF]
Journal of Molecular Biology, 2004 The ubiquitination pathway is the main pathway for protein degradation in eukaryotic cells. The attachment of ubiquitin to a substrate protein is catalyzed by three types of enzymes, namely a ubiquitin activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3). Here, the structure of the human ubiquitin-conjugating enzyme (
Houben, K +5 more
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In vitro Di-ubiquitin Formation Assay and E3 Cooperation Assay
Bio-Protocol, 2022 Ubiquitination is a post-translational modification conserved across eukaryotic species. It contributes to a variety of regulatory pathways, including proteasomal degradation, DNA repair, and cellular differentiation.
Rebecca Burge +3 more
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Dynamic control of selectivity in the ubiquitination pathway revealed by an ASP to GLU substitution in an intra-molecular salt-bridge network [PDF]
, 2012 Ubiquitination relies on a subtle balance between selectivity and promiscuity achieved through specific interactions between ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s).
Bonvin, Alexandre M. J. J. +14 more
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Role of SUMO-1 modification in transcriptional activation [PDF]
, 2012 In unstimulated cells, the transcription factor NF-κB is held in the cytoplasm in an inactive state by IκB inhibitor proteins. Activation of NF--KB is mediated by signal induced degradation of IκBα via the ubiquitin proteasome-dependent pathway ...
Pinto Desterro, Maria Joana
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Structure of the Human FANCL RING-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection [PDF]
, 2014 The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for ubiquitin modification of a substrate. Moreover, the pairing dictates both the substrate choice and the modification type. The molecular details of generic
Miles, Jennifer Anne +3 more
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MALDI-TOF Mass Spectrometry for interrogating ubiquitin enzymes
Frontiers in Molecular Biosciences, 2023 The attachment of ubiquitin to a substrate (ubiquitination or ubiquitylation) impacts its lifetime and regulates its function within the cell. Several classes of enzymes oversee the attachment of ubiquitin to the substrate: an E1 activating enzyme that ...
Virginia De Cesare
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Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]
, 2014 The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G. +20 more
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Transcriptional regulation mediated through the conjugation and deconjugation of the small ubiquitin-like modifiers SUMO-1, SUMO-2, and SUMO-3 [PDF]
, 2012 SUMO-1/2/3 are members of the ubiquitin-like family of protein modifiers. These proteins are covalently attached to numerous proteins in a directed and controlled manner.
Girdwood, David William Haxton
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