The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

DOA1  -  Doa1p

Saccharomyces cerevisiae S288c

Synonyms: Protein DOA1, UFD3, YKL213C, ZZZ4
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

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].

References

  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]
 
WikiGenes - Universities