CUBE INOX WITH HANDLE 9L
- Known as:
- CUBE INOX HANDLE 9L
- Catalog number:
- UCUB-5
- Category:
- -
- Supplier:
- SBS
- Gene target:
- CUBE INOX WITH HANDLE 9L
Related genes to: CUBE INOX WITH HANDLE 9L
- Gene:
- UBE2J1 NIH gene
- Name:
- ubiquitin conjugating enzyme E2 J1
- Previous symbol:
- -
- Synonyms:
- HSPC153, CGI-76, NCUBE1, UBC6
- Chromosome:
- 6q15
- Locus Type:
- gene with protein product
- Date approved:
- 2002-11-26
- Date modifiied:
- 2016-03-14
- Gene:
- UBE2J2 NIH gene
- Name:
- ubiquitin conjugating enzyme E2 J2
- Previous symbol:
- -
- Synonyms:
- Ubc6p, NCUBE2
- Chromosome:
- 1p36.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-11-26
- Date modifiied:
- 2016-03-14
Related products to: CUBE INOX WITH HANDLE 9L
Related articles to: CUBE INOX WITH HANDLE 9L
- The RING-type E3 ubiquitin-protein ligase MuRF1 (also known as TRIM63) plays an important role in skeletal muscle atrophy by targeting contractile proteins. In cellulo, MuRF1 can alternatively interact with four E2 enzymes (UBE2E1, UBE2J1, UBE2J2, or UBE2L3), suggesting different functions or targets for the four MuRF1-E2 complexes. In this article, we studied the interface of these MuRF1-UBE2 complexes based on AlphaFold2 and AlphaFold3 predictions. These predictions revealed the involvement of different residues at the interface of each complex. We confirmed this overall interface difference by the differential sensitivity of MuRF1-E2 complexes to regenerating solutions in surface plasmon resonance experiments. We further confirmed several predictions individually by affinity measurements with point-mutant E2 enzymes and truncated MuRF1. We used the interaction-induced fluorescence change approach with fluorescent MuRF1. Besides canonical E2-RING-type E3 interactions, we were able to identify selective contact points between MuRF1 and its UBE2 partners. Furthermore, in the case of the MuRF1-E2E1 pair, unlike the other MuRF1-E2 pairs, the interaction may also be governed by a domain outside the RING domain. Since the function of RING-type E3s is regulated by E2 enzymes, deciphering the mechanisms of selective recruitment of E2s by MuRF1 paves the way for the development of targeted therapeutics to fight muscle atrophy. - Source: PubMed
Publication date: 2025/02/10
Claustre AgnèsMalige MélodieMacheton MaëlysCombaret LydieLefai EtienneFafournoux PierreTaillandier DanielHenri JulienPolge Cécile - The human Ube2j1 and Ube2j2 are the only ubiquitin-conjugating enzymes (E2s) that are localized to endoplasmic reticulum (ER) through its C-terminal transmembrane domains. Ube2j1 is a known substrate of MAPK signalling pathway and it is phosphorylated at serine-184 during ER stress. Here, we demonstrate that Ube2j1, not Ube2j2 is essential for the recovery of cells from transient ER stress. The ectopic expression of wild-type Ube2j1 and phospho-mimic mutant, Ube2j1 but not phospho-mutant Ube2j1 can recover cells from ER stress. We also found that ubiquitin-ligase (E3), c-IAP1 preferentially interacts with phosphorylated Ube2j1. Moreover, we noticed that phosphorylated Ube2j1 is rapidly degraded by the proteasome during ER stress cell recovery. Taken together, these data suggest that Ube2j1 and its phosphorylation is important for transient ER stress cell recovery and the phosphorylated Ube2j1 is degraded by the proteasome. - Source: PubMed
Publication date: 2017/03/20
Elangovan MuthukumarChong Hae KwanPark Jin HeeYeo Eui JuYoo Yung Joon - Integral membrane and secretory proteins which fail to fold productively are retained in the endoplasmic reticulum and targeted for degradation by cytoplasmic proteasomes. Genetic and biochemical analyses suggest that substrates of this pathway must be dislocated across the membrane of the endoplasmic reticulum (ER) by a process requiring a functional Sec61 complex and multiubiquitinylation. In yeast, the tail-anchored ubiquitin-conjugating enzyme Ubc6p, which is localized to the cytoplasmic surface of the ER, participates in ER-associated degradation (ERAD) of misfolded proteins. Here we describe the identification of two families of mammalian Ubc6p-related proteins. Members of both families are also located in the ER membrane and display a similar membrane topology as the yeast enzyme. Furthermore we show that expression of elevated levels of wild-type and dominant-negative alleles of these components affects specifically ERAD of the alpha subunit of the T-cell receptor and a mutant form of the CFTR protein. Similarly, we describe that the expression level of Ubc6p in yeast is also critical for ERAD, suggesting that the Ubc6p function is highly conserved from yeast to mammals. - Source: PubMed
Lenk UweYu HelenWalter JanGelman Marina SHartmann EnnoKopito Ron RSommer Thomas - Degradation of proteins from the endoplasmic reticulum is fundamental to quality control within the secretory pathway, serves as a way of regulating levels of crucial proteins, and is utilized by viruses to enhance pathogenesis. In yeast two ubiquitin-conjugating enzymes (E2s), UBC6p and UBC7p are implicated in this process. We now report the characterization of murine homologs of these E2s. MmUBC6 is an integral membrane protein that is anchored via its hydrophobic C-terminal tail to the endoplasmic reticulum. MmUBC7, which is not an integral membrane protein, shows significant endoplasmic reticulum colocalization with MmUBC6. Overexpression of catalytically inactive MmUBC7 significantly delayed degradation from the endoplasmic reticulum of two T cell antigen receptor subunits, alpha and CD3-delta, and suggests a role for the ubiquitin conjugating system at the initiation of retrograde movement from the endoplasmic reticulum. These findings also implicate, for the first time, a specific E2 in degradation from the endoplasmic reticulum in mammalian cells. - Source: PubMed
Publication date: 2001/02/02
Tiwari SWeissman A M