Proteasome subunit Rpn13 is a novel ubiquitin receptor
By K. Husnjak, S. Elsasser, Naixia Zhang, Xiang Chen, Leah Randles, Yuan Shi, Kay Hofmann, K. Walters, D. Finley, Ivan Dikic. Nature, 2008
700 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/39875271835dbb9ebfdf8aa23b1a0598c496a018
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Epidemiology
In Molecular Biology
Citations in the corpus
- One step at a time: endoplasmic reticulum-associated degradation (2008, background): “Recent data strongly suggest that Rpn13 mediates the highest affinity binding, and its position in the proteasome is consistent with it having a key role during substrate degradatio”
- A role for ubiquitin in selective autophagy. (2009, background): “Conjugated Ub moieties are recognized by Ubbinding domain (UBD)-containing proteins (Hicke et al., 2005), and similarly, we expect that autophagy-specific UBLs, via noncovalent interactions, may recruit components of signaling complexes to the nascent autophagosomes and/or provide a means of…”
- Atypical ubiquitin chains: new molecular signals (2008, background): “More recently, rpN13/arM1 was identified as a new ub receptor at the proteasome and shown to stoichiometrically bind to Lys 48- linked diub through its pleckstrin-like receptor for ubiquitin (pru) domain (Husnjak et al, 2008; Schreiner et al, 2008).”
- Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “In addition to interacting with and activating Uch37 hydrolysis of Ub-AMC, Adrm1 also interacts with the S1/PSMD1 subunit and polyubiquitin through different surfaces of its N-terminal domain (137, 146).”
- Complete subunit architecture of the proteasome regulatory particle (2012, positive): “However, knockout studies have shown that ubiquitin chains are not required to bind to multiple receptors simultaneously 38 .”
- Targeting the ubiquitin system in cancer therapy (2009, background): “, preventing the recognition of ubiquitylated substrates by UBDs present in the proteasome receptors RPN10 and RPN13, as well as the shuttling receptor RAD23 that targets the same surfac”
- Structure and Function of the 26S Proteasome (2018, background): “However, each receptor provides unique contributions to linkage-type preferences, with intrinsic receptors preferring K48-linked chains over other linkage types, but the biological relevance of these overall preferences remains unclear (19, 124, 131, 140, 141).”
- Ubiquitin-binding domains — from structures to functions (2009, background): “These properties of the PRU domain contribute to its higher affinity for monoubiquiti”
- Origin and Function of Ubiquitin-like Protein Conjugation (2009, background): “Multiple polyubiquitin receptors are present within the proteasom”
- Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “Proteasomes from some tissues contain Rpn13 in excess over Uch37, and would thus have an unoccupied Uch37 binding site available to activate.”
- Selective autophagy: ubiquitin-mediated recognition and beyond (2010, background): “Recognition of a genuine substrate by the proteasome is mediated by specific receptor subunits that contain dedicated ubiquitin-interacting motif”
- The ubiquitin code. (2012, background): “Thus, Lys63-linked chains can trigger proteolysis, yet efficient targeting to such as the specific localization of effector proteins. www.annualreviews.org • The Ubiquitin Code 217”
- Post-translational modifications in signal integration (2010, background): “), plekstrin homology–like (for example, the PRU domain of RPN13 (ref”
- The Logic of the 26S Proteasome. (2017, positive): “, 2006) and binds Ub chains via its PRU domain (Husnjak et al., 2008).”