Correction to: Adaptors as the regulators of HECT ubiquitin ligases
نویسندگان
چکیده
منابع مشابه
Evolution of Plant HECT Ubiquitin Ligases
HECT ubiquitin ligases are key components of the ubiquitin-proteasome system, which is present in all eukaryotes. In this study, the patterns of emergence of HECT genes in plants are described. Phylogenetic and structural data indicate that viridiplantae have six main HECT subfamilies, which arose before the split that separated green algae from the rest of plants. It is estimated that the comm...
متن کاملA Tunable Brake for HECT Ubiquitin Ligases.
The HECT E3 ligases ubiquitinate numerous transcription factors and signaling molecules, and their activity must be tightly controlled to prevent cancer, immune disorders, and other diseases. In this study, we have found unexpectedly that peptide linkers tethering WW domains in several HECT family members are key regulatory elements of their catalytic activities. Biochemical, structural, and ce...
متن کاملMammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects.
Members of the HECT family of E3 ubiquitin-protein ligases are characterized by a C-terminal HECT domain that catalyzes the covalent attachment of ubiquitin to substrate proteins and by N-terminal extensions of variable length and domain architecture that determine the substrate spectrum of a respective HECT E3. Since their discovery in 1995, it has become clear that deregulation of distinct HE...
متن کاملPeptide and small molecule inhibitors of HECT-type ubiquitin ligases.
The human genome encodes several hundred E3 ubiquitin ligases containing RING domains, and around 28 containing HECT domains. These enzymes catalyze the transfer of ubiquitin from E2 enzyme thioesters to a huge range of substrates and play crucial roles in many cellular functions. This makes them attractive potential therapeutic targets. However, they have proven difficult to inhibit: very few ...
متن کاملActivity‐Based Probes for HECT E3 Ubiquitin Ligases
Activity-based probes (ABPs) have been used to dissect the biochemical/structural properties and cellular functions of deubiquitinases. However, their utility in studying cysteine-based E3 ubiquitin ligases has been limited. In this study, we evaluate the use of ubiquitin-ABPs (Ub-VME and Ub-PA) and a novel set of E2-Ub-ABPs on a panel of HECT E3 ubiquitin ligases. Our in vitro data show that u...
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ژورنال
عنوان ژورنال: Cell Death & Differentiation
سال: 2021
ISSN: 1350-9047,1476-5403
DOI: 10.1038/s41418-021-00737-8