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Gene Review

YND1  -  Ynd1p

Saccharomyces cerevisiae S288c

Synonyms: ADPase, APY1, ATP-diphosphatase, ATP-diphosphohydrolase, Adenosine diphosphatase, ...
 
 
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Disease relevance of YND1

 

High impact information on YND1

  • However, Ynd1p apyrase activity was not required for E4orf4-induced toxicity [1].
  • By using a two-hybrid screen, we found that an activator subunit (Vma13p) of yeast vacuolar H(+)-ATPase (V-ATPase) binds to the cytoplasmic domain of Ynd1p, a yeast ectoapyrase [2].
  • YND1, a homologue of GDA1, encodes membrane-bound apyrase required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae [3].
  • The overexpression of the YND1 gene in the gda1 null mutant caused a significant increase in microsomal membrane-bound nucleoside phosphatase activity with a luminal orientation [3].
  • The activity was equally high toward ADP/ATP, GDP/GTP, and UDP/UTP and approximately 50% less toward CDP/CTP and thiamine pyrophosphate, but there was no activity toward GMP, indicating that the Ynd1 protein belongs to the apyrase family [3].
 

Biological context of YND1

  • The overexpression of the YND1 gene complemented some glycosylation defects in Deltagda1 disruptants, suggesting a partially redundant function of yeast apyrase and GDPase [3].
  • The gene for the open reading frame YER005w that is homologous to yeast Golgi GDPase encoded by the GDA1 gene was cloned and named YND1 [3].
  • A similar increase in the apyrase activity of Ynd1p was found in a vma1Delta mutant, in which the catalytic subunit A of V-ATPase is missing, and the membrane peripheral subunits including Vma13p are dissociated from the membranes [2].
  • ATP-diphosphohydrolase (apyrase) catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates in the presence of divalent cations [4].
 

Associations of YND1 with chemical compounds

  • We show that deletion of YND1, like deletion of GDA1, alters the sphingolipid profiles, suggesting that changes in sphingolipids compensate for lethality produced by changes in sterol composition and abundance [5].
 

Other interactions of YND1

  • The results suggested that Ynd1p and Cdc55p share a common downstream target whose balanced modulation by the two E4orf4 partners is crucial to viability [1].
  • Interaction of Ynd1p with Vma13p was demonstrated by direct binding and co-immunoprecipitation [2].

References

  1. YND1 interacts with CDC55 and is a novel mediator of E4orf4-induced toxicity. Maoz, T., Koren, R., Ben-Ari, I., Kleinberger, T. J. Biol. Chem. (2005) [Pubmed]
  2. Regulation of yeast ectoapyrase ynd1p activity by activator subunit Vma13p of vacuolar H+-ATPase. Zhong, X., Malhotra, R., Guidotti, G. J. Biol. Chem. (2000) [Pubmed]
  3. YND1, a homologue of GDA1, encodes membrane-bound apyrase required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae. Gao, X.D., Kaigorodov, V., Jigami, Y. J. Biol. Chem. (1999) [Pubmed]
  4. Methylotrophic yeast Pichia pastoris as a host for production of ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum). Nourizad, N., Ehn, M., Gharizadeh, B., Hober, S., Nyrén, P. Protein Expr. Purif. (2003) [Pubmed]
  5. Cumulative mutations affecting sterol biosynthesis in the yeast Saccharomyces cerevisiae result in synthetic lethality that is suppressed by alterations in sphingolipid profiles. Valachovic, M., Bareither, B.M., Shah Alam Bhuiyan, M., Eckstein, J., Barbuch, R., Balderes, D., Wilcox, L., Sturley, S.L., Dickson, R.C., Bard, M. Genetics (2006) [Pubmed]
 
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