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UBC6 Ubc6p

UBC6, Ubc6p
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, UBC7, V1a, Sec61, HRD1
Papers on UBC6
An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme.
Hochstrasser et al., New Haven, United States. In J Biol Chem, 2011
Yeast Doa10 is a polytopic membrane ubiquitin ligase (E3) that along with its cognate ubiquitin-conjugating enzymes (E2s), Ubc7 and the C-terminally membrane-anchored Ubc6, makes a major contribution to ER-associated degradation.
HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation.
GeneRIF
Lehner et al., Cambridge, United Kingdom. In Proc Natl Acad Sci U S A, 2011
data support a physiological role for HRD1 and UBE2J1 in the homeostatic regulation of MHC class I assembly and expression
Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates.
GeneRIF
Hansen et al., Saint Louis, United States. In J Cell Biol, 2009
Ube2j2 is the primary cellular E2 recruited by the mK3 ligase, and this E2-E3 pair is capable of conjugating Ub on lysine or serine residues of substrates.
Validation of reference genes for quantitative expression analysis by real-time RT-PCR in Saccharomyces cerevisiae.
Parrou et al., Toulouse, France. In Bmc Mol Biol, 2008
Using the algorithm geNorm, ALG9, TAF10, TFC1 and UBC6 turned out to be genes whose expression remained stable, independent of the growth conditions and the strain backgrounds tested in this study.
Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.
Michaelis et al., Baltimore, United States. In J Biol Chem, 2008
As shown previously, we observe that the ER-localized ubiquitin E2 (Ubc6p, Ubc7p, and Cue1p) and E3 (Doa10p) machinery involved in ER-associated degradation (ERAD) are also responsible for the degradation of the cytosolic substrate Ura3p-CL1.
Human homologs of Ubc6p ubiquitin-conjugating enzyme and phosphorylation of HsUbc6e in response to endoplasmic reticulum stress.
GeneRIF
Rommens et al., Toronto, Canada. In J Biol Chem, 2006
Ubc6e is phosphorylated in response to endoplasmic reticulum stress
An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery.
Canessa et al., New Haven, United States. In Proc Natl Acad Sci U S A, 2006
We determined that the Ub-conjugating UBC6 and UBC7 and the Ub ligase HRD1 are the ER-associated Ub enzymes that mediate degradation of Sgk1; thus, Sgk1 has been identified as a cytosolic substrate for mammalian HRD1.
Vacuolar degradation of rat liver CYP2B1 in Saccharomyces cerevisiae: further validation of the yeast model and structural implications for the degradation of mammalian endoplasmic reticulum P450 proteins.
Correia et al., San Francisco, United States. In Mol Pharmacol, 2005
No comparable CYP2B1 stabilization was detected in yeast genetically deficient in the ER Ub-conjugating enzyme Ubc6p or Ubc7p or defective in 19S proteasomal subunit Hrd2p.
Endoplasmic reticulum-associated degradation of the human type 2 iodothyronine deiodinase (D2) is mediated via an association between mammalian UBC7 and the carboxyl region of D2.
Bianco et al., Boston, United States. In Mol Endocrinol, 2003
Mammalian UBC6 (MmUBC6) does not directly associate with D2 but can associate with a complex containing UBC7 and D2.
Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+.
Wojcikiewicz et al., Syracuse, United States. In J Biol Chem, 2003
In the present study we have examined the enzymology of ubiquitination of endogenous InsP3Rs in muscarinic agonist-stimulated SH-SY5Y human neuroblastoma cells, focusing our attention on two mammalian E2s, MmUbc6 and MmUbc7, that have been implicated in endoplasmic reticulum-associated degradation (ERAD) and are homologous to the yeast ERAD E2s, Ubc6p and Ubc7p.
Mutant membrane protein of the budding yeast spindle pole body is targeted to the endoplasmic reticulum degradation pathway.
Winey et al., Boulder, United States. In Genetics, 2002
Both mps2-1 and ndc1-1 are also suppressed by disruption of UBC7 or its partner, UBC6.
Ubc6p and ubc7p are required for normal and substrate-induced endoplasmic reticulum-associated degradation of the human selenoprotein type 2 iodothyronine monodeiodinase.
Bianco et al., Boston, United States. In Mol Endocrinol, 2002
Expression of CysD2 in yeast strains that lack the ubiquitin conjugases Ubc6p or Ubc7p stabilized CysD2 half-life by markedly reducing CysD2 ubiquitination, whereas no difference was detected in Ubc1p-deficient mutants.
A role for mammalian Ubc6 homologues in ER-associated protein degradation.
Sommer et al., Berlin, Germany. In J Cell Sci, 2002
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.
Role of Cue1p in ubiquitination and degradation at the ER surface.
Impact
Sommer et al., Berlin, Germany. In Science, 1998
Moreover, ubiquitination by Cue1p-assembled Ubc7p and Ubc6p was a prerequisite for retrograde transport of lumenal substrates out of the ER, which suggests that ubiquitination is mechanistically integrated into the ER degradation process.
Endoplasmic reticulum degradation: reverse protein flow of no return.
Review
Wolf et al., Berlin, Germany. In Faseb J, 1997
Representatives of ER membrane-bound ubiquitin-conjugating enzymes, Ubc6p and Cue1p/Ubc7p, have been identified in yeast.
A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum.
Impact
Jentsch et al., Tübingen, Germany. In Nature, 1993
This enzyme, UBC6, localizes to the endoplasmic reticulum (ER), with the catalytic domain facing the cytosol.
Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor.
Impact
Hochstrasser et al., Chicago, United States. In Cell, 1993
The UBC6/UBC7-containing complex targets the Deg1 degradation signal of alpha 2, a conclusion underscored by the finding that UBC6 is encoded by DOA2, a gene previously implicated in Deg1-mediated degradation.
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