Building ubiquitin chains: E2 enzymes at work

By Y. Ye, M. Rapé. Nature reviews. Molecular cell biology, 2009

1,039 citations recorded by the source corpus.

The modification of proteins with ubiquitin chains can change their localization, activity and/or stability. Although ubiquitylation requires the concerted action of ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s), it is the E2s that have recently emerged as key mediators of chain assembly. These enzymes are able to govern the switch from ubiquitin chain initiation to elongation, regulate the processivity of chain formation and establish the topology of assembled chains, thereby determining the consequences of ubiquitylation for the modified proteins.

Subfields: Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e8324db196f5eef7c5f93d73b087269eabd6f7e6

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Citations in the corpus

Systematic and quantitative assessment of the ubiquitin modified proteome (2011, positive): “In this pathway, ubiquitin is activated and transferred to substrates via an E1-E2-E3 cascade (Ye and Rape, 2009).”
The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “The existence of these problems is closely related to the technical deficiency in detecting the length of the polyubiquitin chain; thus, useful technology to address the looming question is the key to unlocking new areas of UPS.”
Quantitative proteomics reveal a feed-forward model for mitochondrial PARKIN translocation and UB chain synthesis (2014, positive): “…by PINK1 dramatically activates its UB ligase activity and synthesis of K6, K11, K48, and K63 chain linkage types, providing, to our knowledge, the first example of a RING-HECT hybrid E3 that can intrinsically produce four specific linkage types (Kulathu and Komander, 2012; Ye and Rape, 2009).”
Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15 (2017, background): “This is likely either the consequence of fewer representative peptides, given its small size (108 amino acids), or its low affinity for the cullin scaffold (28).”
Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis (2013, background): “E2 enzymes play an important role in dictating the length and specific linkages of Ub chains and the processivity of the reaction (22).”