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Gene Review

DOA1  -  Doa1p

Saccharomyces cerevisiae S288c

Synonyms: Protein DOA1, UFD3, YKL213C, ZZZ4
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High impact information on DOA1


Biological context of DOA1

  • While searching for regulators of virulence attributes of the human-pathogenic fungus Candida albicans, a gene was identified similar to the genes encoding the mammalian phospholipase A2-activating protein (PLAP) and the Saccharomyces cerevisiae protein Doa1, which is known to play a key role during ubiquitin (Ub)-dependent protein degradation [4].
  • Role of Doa1 in the Saccharomyces cerevisiae DNA damage response [3].
  • Both zzz4-1 and a deletion of ZZZ4 confer resistance to all five of the agents tested, suggesting that signal transduction may be involved in the response of these cells to volatile anesthetics [5].
  • Here, we describe Saccharomyces cerevisiae Doa1, which helps to control the damage response by channeling ubiquitin from the proteosomal degradation pathway into pathways that mediate altered DNA replication and chromatin modification [3].
  • Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues [6].

Physical interactions of DOA1

  • Herein, we demonstrate that Cdc48 interacts directly with the C-terminal PUL domain of Doa1 [7].

Regulatory relationships of DOA1

  • Mutations in Doa1 that block Hse1 binding but not Ub binding do not alter Ub levels but do result in the missorting of the MVB cargo GFP-Cps1 [8].

Other interactions of DOA1

  • DOA1 and CDC48 mutations are epistatic, suggesting that their interaction is physiologically relevant [7].
  • These data suggest that DOA1 of C. albicans, like its orthologue in S. cerevisiae, is associated with Ub-mediated proteolysis and has multiple functions [4].
  • They were identified as Ubp14, the yeast ortholog of Isopeptidase T, and Ufd3, a member of the ubiquitin-fusion degradation pathway with unknown function [6].


  1. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Rumpf, S., Jentsch, S. Mol. Cell (2006) [Pubmed]
  2. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. Ghislain, M., Dohmen, R.J., Levy, F., Varshavsky, A. EMBO J. (1996) [Pubmed]
  3. Role of Doa1 in the Saccharomyces cerevisiae DNA damage response. Lis, E.T., Romesberg, F.E. Mol. Cell. Biol. (2006) [Pubmed]
  4. Multiple functions of DOA1 in Candida albicans. Kunze, D., Maccallum, D., Odds, F.C., Hube, B. Microbiology (Reading, Engl.) (2007) [Pubmed]
  5. Molecular genetic analysis of volatile-anesthetic action. Keil, R.L., Wolfe, D., Reiner, T., Peterson, C.J., Riley, J.L. Mol. Cell. Biol. (1996) [Pubmed]
  6. Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues. Russell, N.S., Wilkinson, K.D. Biochemistry (2004) [Pubmed]
  7. Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain. Mullally, J.E., Chernova, T., Wilkinson, K.D. Mol. Cell. Biol. (2006) [Pubmed]
  8. DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into multivesicular bodies. Ren, J., Pashkova, N., Winistorfer, S., Piper, R.C. J. Biol. Chem. (2008) [Pubmed]
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