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Gene Review

SPT23  -  Spt23p

Saccharomyces cerevisiae S288c

Synonyms: Protein SPT23, YKL020C
 
 
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High impact information on SPT23

  • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone [1].
  • SPT23 and MGA2 are relatives of mammalian NF-kappaB and control unsaturated fatty acid levels [2].
  • Previous studies have suggested that the pathway regulating OLE1 expression by unsaturated fatty acids may involve Mga2p and Spt23p, two structurally and functionally related proteins [3].
  • Spt23p appears to be a rate-limiting component required for functional HIS4 expression of his4-912delta, a promoter insertion mutation induced by the Ty1-912 long terminal repeat [4].
  • A 50-amino-acid region in the N terminus of the predicted Spt23p protein is necessary and sufficient for the transactivation and necessary for suppression of Ty1-induced mutations and the essential function of Spt23p [4].
 

Biological context of SPT23

 

Anatomical context of SPT23

 

Associations of SPT23 with chemical compounds

 

Regulatory relationships of SPT23

  • Deletion of this motif abrogates Rsp5p-induced ubiquitination of Spt23p in vitro and reduces ubiquitination of the Spt23p precursor in yeast [10].
 

Other interactions of SPT23

  • SPT23/MGA2 and the SNF/SWI genes affect transcription of certain target genes in similar ways [4].
  • The control of OLE1 gene expression appears to mediated through the ER membrane proteins Spt23p and Mga2p [11].
  • Although previous studies documented an Rsp5p-Spt23p association in cells, very little is known about the nature of this interaction [10].
  • SPT23 is synthesized as an inactive, ER membrane-anchored precursor that is activated by regulated ubiquitin/proteasome-dependent processing (RUP) [1].
 

Analytical, diagnostic and therapeutic context of SPT23

References

  1. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H., Jentsch, S. Cell (2001) [Pubmed]
  2. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H.D., Jentsch, S. Cell (2000) [Pubmed]
  3. MGA2 is involved in the low-oxygen response element-dependent hypoxic induction of genes in Saccharomyces cerevisiae. Jiang, Y., Vasconcelles, M.J., Wretzel, S., Light, A., Martin, C.E., Goldberg, M.A. Mol. Cell. Biol. (2001) [Pubmed]
  4. Genetic redundancy between SPT23 and MGA2: regulators of Ty-induced mutations and Ty1 transcription in Saccharomyces cerevisiae. Zhang, S., Burkett, T.J., Yamashita, I., Garfinkel, D.J. Mol. Cell. Biol. (1997) [Pubmed]
  5. MGA2 and SPT23 are modifiers of transcriptional silencing in yeast. Dula, M.L., Holmes, S.G. Genetics (2000) [Pubmed]
  6. MGA2 or SPT23 is required for transcription of the delta9 fatty acid desaturase gene, OLE1, and nuclear membrane integrity in Saccharomyces cerevisiae. Zhang, S., Skalsky, Y., Garfinkel, D.J. Genetics (1999) [Pubmed]
  7. Molecular characterization of the SPT23 gene: a dosage-dependent suppressor of Ty-induced promoter mutations from Saccharomyces cerevisiae. Burkett, T.J., Garfinkel, D.J. Yeast (1994) [Pubmed]
  8. The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Hitchcock, A.L., Krebber, H., Frietze, S., Lin, A., Latterich, M., Silver, P.A. Mol. Biol. Cell (2001) [Pubmed]
  9. Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90. Shcherbik, N., Zoladek, T., Nickels, J.T., Haines, D.S. Curr. Biol. (2003) [Pubmed]
  10. A single PXY motif located within the carboxyl terminus of Spt23p and Mga2p mediates a physical and functional interaction with ubiquitin ligase Rsp5p. Shcherbik, N., Kee, Y., Lyon, N., Huibregtse, J.M., Haines, D.S. J. Biol. Chem. (2004) [Pubmed]
  11. Regulation of long chain unsaturated fatty acid synthesis in yeast. Martin, C.E., Oh, C.S., Jiang, Y. Biochim. Biophys. Acta (2007) [Pubmed]
 
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