2012
DOI: 10.1016/j.str.2012.09.020
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Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

Abstract: Recognition of ubiquitin and polyubiquitin chains by ubiquitin-binding domains (UBDs) is vital for ubiquitin-mediated signaling pathways. The endoplasmic reticulum resident RING finger ubiquitin ligase (E3) gp78 regulates critical proteins via the ubiquitin-proteasome system to maintain cellular homeostasis and includes a UBD known as the CUE domain, which is essential for function. A probable role of this domain is to recognize ubiquitin modified substrates, enabling gp78 to assemble polyubiquitin chains on t… Show more

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Cited by 33 publications
(86 citation statements)
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“…Protein ubiqutination has emerged as a key mechanism involved in growth and development as well as immunity in animals and plants (Liu et al ., ; You et al ., ). Recognition of ubiquitin or specific ubiquitin chains by ubiquitin‐binding domains (UBDs) is vital for deciphering ubiquitin‐mediated signalling pathways (Liu et al ., ). Among a handful of types of characterized UBDs, the coupling of ubiquitin conjugation to endoplasmic reticulum (ER) degradation (CUE) domains consisting of 42–43 amino acid sequences have been identified and characterized based on similarity to the region of the yeast Cue1 protein, which is implicated in yeast ER‐associated degradation (ERAD; Shih et al ., ); however, their roles in ERAD remain poorly understood (Li et al ., ; Liu et al ., ; Shideler et al ., ).…”
Section: Introductionmentioning
confidence: 97%
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“…Protein ubiqutination has emerged as a key mechanism involved in growth and development as well as immunity in animals and plants (Liu et al ., ; You et al ., ). Recognition of ubiquitin or specific ubiquitin chains by ubiquitin‐binding domains (UBDs) is vital for deciphering ubiquitin‐mediated signalling pathways (Liu et al ., ). Among a handful of types of characterized UBDs, the coupling of ubiquitin conjugation to endoplasmic reticulum (ER) degradation (CUE) domains consisting of 42–43 amino acid sequences have been identified and characterized based on similarity to the region of the yeast Cue1 protein, which is implicated in yeast ER‐associated degradation (ERAD; Shih et al ., ); however, their roles in ERAD remain poorly understood (Li et al ., ; Liu et al ., ; Shideler et al ., ).…”
Section: Introductionmentioning
confidence: 97%
“…In animals, some CUE domain‐containing (CUEDC) proteins have been implicated in programmed cell death (PCD) and immunity. For examples, the CUEDC protein, ERAD E3 gp78, is a regulator of liver homeostasis and a tumour suppressor in liver, and its CUE domain interacts with ubiquitin and diubiquitin and functions to facilitate substrate binding and processivity in ubiquitination (Liu et al ., ; Zhang et al ., ); another CUEDC protein, CUEDC2, suppresses glioma tumorigenicity by inhibiting the activation of STAT3 and NF‐κB, and its CUE domain is essential for functional interactions with both monoubiquitin and polyubiquitin (Li et al ., ). In plants, the reported CUECD proteins are the duplicated pair of Arabidopsis RING‐finger E3 ligases, RIN2 and RIN3, which each possess a RING‐finger domain in association with a CUE domain; however, the CUE domain was rarely characterized for its roles in the E3 ligases (Kawasaki et al ., ).…”
Section: Introductionmentioning
confidence: 99%
“…The ability of the NESTA algorithm to reconstruct weak NOESY peaks in a 4D CCNOESY spectrum was examined for a small protein domain, CUE, from the ubiquitin E3 ligase gp78 (Liu et al 2012). The sample was 2 H, 13 C, 15 N-labeled with the exception that Ileδ1, Leu, Val methyl groups were protonated ( 1 H).…”
Section: Resultsmentioning
confidence: 99%
“…Experimental data were collected on three different proteins: (1) a 1 mM sample of the 8 kDa CUE domain containing residues 453–504 from human gp78 (Liu et al 2012); (2) a 330 μM sample of the 15 kDa PH domain of ASAP1, which contains residues 339–451 (Luo et al 2008); and (3) a 400 μM sample of the 32 kDa two domain construct (ZA) of ASAP1 containing residues 441–724 (Luo et al 2008). Isotope labeling was performed by expressing and purifying the proteins from E. coli using standard techniques to produce either uniform 13 C, 15 N-labeled protein, uniform 2 H, 13 C, 15 N-labeled protein (DCN), or uniform 2 H, 13 C, 15 N, 13 C 1 H 3 -methyl (Ileδ1, Leu, Val) labeled protein (DCN-ILV) or 2 H, 15 N, 13 C 1 H 3 -methyl (Ileδ1, Leu, Val) labeled protein (DC methyl N-ILV).…”
Section: Methodsmentioning
confidence: 99%
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