High impact information on UBC6

• This suggests that UBC6 may mediate selective degradation of ER membrane proteins and that the protein translocation defect of sec61 may be caused by proteolysis of components of a structurally distorted mutant translocation apparatus [1].
• Doa10 functions with two E2s, Ubc6 and Ubc7, to ubiquitinate Deg1-bearing substrates, and it is also required for the degradation of at least one ER membrane protein [2].
• UBC6 lacks a lumenal domain and contains no known endoplasmic reticulum retention signals [3].
• The basis for the transmembrane domain-mediated subcellular targeting of UBC6 was evaluated by lengthening the wild type UBC6 hydrophobic segment from 17 to 21 amino acids, which resulted in re-targeting to the Golgi complex [3].
• The similarity of this region with sequences contained within the tails of the UBC1 and UBC6 enzymes suggests that these tails may function in a similar manner [4].

Biological context of UBC6

• The expression of the sec61 mutant phenotype requires both the activity of UBC6 and its localization at the ER membrane [1].
• This enzyme, UBC6, localizes to the endoplasmic reticulum (ER), with the catalytic domain facing the cytosol. ubc6 loss-of-function mutants suppress the protein translocation defect caused by a mutation in SEC61, which encodes a key component of a multisubunit protein translocation apparatus of the ER [1].
• Together with yeast UBC6 these proteins constitute a distinct family of UBCs sharing a conserved noncanonical active site sequence and a C-terminal transmembrane domain [5].

Other interactions of UBC6

• Both mps2-1 and ndc1-1 are also suppressed by disruption of UBC7 or its partner, UBC6 [6].

References