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Gene Review

AQY1  -  Aqy1p

Saccharomyces cerevisiae S288c

Synonyms: AQY1-2, Aquaporin-1, P9677.5, YPR192W
 
 
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Disease relevance of AQY1

  • Perhaps as a result, there was no difference between the virulence of C. albicans wild-type and aqy1 null strains in a murine model for systemic candidiasis [1].
 

High impact information on AQY1

  • Here, we show that expression of AQY1 is stimulated during sporulation and that the Aqy1 protein is detectable exclusively in spore membranes [2].
  • Taken together, we demonstrate a functional role of an aquaporin in gametogenesis, as well as in the formation of durable structures such as spores, a role that may have wider biological and medical implications [2].
  • The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2 [3].
  • Comparison of these strains revealed that the aquaporin null cells were more aggregated and their surface was more hydrophobic [3].
  • As a result, the aquaporin null cells were more flocculent and more efficient at haploid invasive growth [3].
 

Biological context of AQY1

 

Anatomical context of AQY1

  • AQY1 from laboratory and wild-type strains of Saccharomyces were expressed in Xenopus oocytes to determine the coefficients of osmotic water permeability (Pf) [4].
  • Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species [4].
  • Pf measurements in yeast spheroplasts confirmed the presence of functional water channels in Sigma1278b and a pharmacological study indicated that this strain contains at least a second functional aquaporin [7].
 

Associations of AQY1 with chemical compounds

  • We showed that the defect in the yeast glycerol plasma membrane transporter is complemented by a plant cDNA encoding the aquaporin BobTIP1;1 which is localized in the vacuolar membrane of the complemented yeast cells [8].
  • We have now obtained direct evidence that selected aquaporin homologues from plants and mammals have the capacity to channel H(2)O(2) across membranes [9].
 

Analytical, diagnostic and therapeutic context of AQY1

References

  1. Aquaporin in Candida: characterization of a functional water channel protein. Carbrey, J.M., Cormack, B.P., Agre, P. Yeast (2001) [Pubmed]
  2. The Saccharomyces cerevisiae aquaporin Aqy1 is involved in sporulation. Sidoux-Walter, F., Pettersson, N., Hohmann, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  3. Aquaporins in Saccharomyces: Characterization of a second functional water channel protein. Carbrey, J.M., Bonhivers, M., Boeke, J.D., Agre, P. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  4. Aquaporins in Saccharomyces. Genetic and functional distinctions between laboratory and wild-type strains. Bonhivers, M., Carbrey, J.M., Gould, S.J., Agre, P. J. Biol. Chem. (1998) [Pubmed]
  5. Aquaporin expression correlates with freeze tolerance in baker's yeast, and overexpression improves freeze tolerance in industrial strains. Tanghe, A., Van Dijck, P., Dumortier, F., Teunissen, A., Hohmann, S., Thevelein, J.M. Appl. Environ. Microbiol. (2002) [Pubmed]
  6. Phenotypes of aquaporin mutants in genetically altered mice. Wasson, K. Comp. Med. (2006) [Pubmed]
  7. Molecular and functional study of AQY1 from Saccharomyces cerevisiae: role of the C-terminal domain. Laizé, V., Gobin, R., Rousselet, G., Badier, C., Hohmann, S., Ripoche, P., Tacnet, F. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  8. The yeast osmosensitive mutant fps1Delta transformed by the cauliflower BobTIP1;1 aquaporin withstand a hypo-osmotic shock. Prudent, S., Marty, F., Charbonnier, M. FEBS Lett. (2005) [Pubmed]
  9. Membrane transport of hydrogen peroxide. Bienert, G.P., Schjoerring, J.K., Jahn, T.P. Biochim. Biophys. Acta (2006) [Pubmed]
  10. Phosphorylation of aquaporin PvTIP3;1 defined by mass spectrometry and molecular modeling. Daniels, M.J., Yeager, M. Biochemistry (2005) [Pubmed]
 
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