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STE13  -  Ste13p

Saccharomyces cerevisiae S288c

Synonyms: DPAP A, Dipeptidyl aminopeptidase A, YCI1, YOR219C, YOR50-9, ...
 
 
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High impact information on STE13

  • The cloned STE13 gene on a plasmid causes yeast cells to overproduce DPAPase A severalfold [1].
  • Absence of DPAPase A and the other phenotypes of a ste13 lesion cosegregate in genetic crosses [1].
  • Lack of the Kex1 protease but not the Ste13 protease results in similar defects [2].
  • The clathrin adaptor complex 1 directly binds to a sorting signal in Ste13p to reduce the rate of its trafficking to the late endosome of yeast [3].
  • Using a new assay for membrane fusion between late Golgi/endosomal compartments, we have reconstituted a rapid, robust homotypic fusion reaction between membranes containing Kex2p and Ste13p, two enzymes resident in the yeast trans-Golgi network (TGN) [4].
 

Biological context of STE13

  • Isolation and DNA sequence of the STE13 gene encoding dipeptidyl aminopeptidase [5].
  • The STE13 open reading frame of 931 amino acids contains a putative membrane-spanning segment near its amino terminus and is 31% identical to a second yeast dipeptidyl aminopeptidase (DAP2) [5].
  • Amino acid sequence analysis revealed that the N terminus of mature Kex2 protease is created by a potentially autoproteolytic cleavage at Lys108-Arg109, prior to the domain homologous to subtilisin, followed by trimming of Leu-Pro and Val-Pro dipeptides by the Ste13 dipeptidyl aminopeptidase [6].
  • Golgi-to-late endosome trafficking of the yeast pheromone processing enzyme Ste13p is regulated by a phosphorylation site in its cytosolic domain [7].
 

Anatomical context of STE13

 

Associations of STE13 with chemical compounds

  • To investigate the mechanism of localization of yeast TGN proteins, we used the heterologous protein A-ALP (consisting of the cytosolic domain of dipeptidyl aminopeptidase A [DPAP A] fused to the transmembrane and luminal domains of the vacuolar protein alkaline phosphatase [ALP]), which localizes to the yeast TGN [11].
 

Physical interactions of STE13

  • Using an in vitro binding assay, Grd19p was found to interact physically with the cytosolic domain of DPAP A [12].
  • Our findings indicate that DPAP A is aberrantly transported to the cell surface but GDPase is not [13].
 

Other interactions of STE13

  • In mutant cells carrying a temperature-sensitive allele of CHC1 (chc1-ts), alpha-factor precursor appears in the culture medium within 15 min, and Kex2p and DPAP A reach the cell surface within 30 min, after imposing the nonpermissive temperature [13].
  • Further analysis of the Kex2p TLS revealed similarity to the Ste13p TLS [14].
  • In this study, we report the identification of a new gene, GRD19, involved in the localization of the model late-Golgi membrane protein A-ALP (consisting of the cytosolic domain of dipeptidyl aminopeptidase A [DPAP A] fused to the transmembrane and lumenal domains of the alkaline phosphatase [ALP]), which localizes to the yeast TGN [12].
  • Regulation of alpha-factor production in Saccharomyces cerevisiae: a-factor pheromone-induced expression of the MF alpha 1 and STE13 genes [15].
 

Analytical, diagnostic and therapeutic context of STE13

References

  1. Yeast alpha factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Julius, D., Blair, L., Brake, A., Sprague, G., Thorner, J. Cell (1983) [Pubmed]
  2. The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating. Heiman, M.G., Engel, A., Walter, P. J. Cell Biol. (2007) [Pubmed]
  3. The clathrin adaptor complex 1 directly binds to a sorting signal in Ste13p to reduce the rate of its trafficking to the late endosome of yeast. Foote, C., Nothwehr, S.F. J. Cell Biol. (2006) [Pubmed]
  4. The Tlg SNARE complex is required for TGN homotypic fusion. Brickner, J.H., Blanchette, J.M., Sipos, G., Fuller, R.S. J. Cell Biol. (2001) [Pubmed]
  5. Isolation and DNA sequence of the STE13 gene encoding dipeptidyl aminopeptidase. Anna-Arriola, S.S., Herskowitz, I. Yeast (1994) [Pubmed]
  6. Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease. Brenner, C., Fuller, R.S. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  7. Golgi-to-late endosome trafficking of the yeast pheromone processing enzyme Ste13p is regulated by a phosphorylation site in its cytosolic domain. Johnston, H.D., Foote, C., Santeford, A., Nothwehr, S.F. Mol. Biol. Cell (2005) [Pubmed]
  8. Localization of dipeptidyl aminopeptidase yscIV in the plasma membrane of Saccharomyces cerevisiae. Bordallo, C., Cueva, R., Suárez Rendueles, P. J. Gen. Microbiol. (1990) [Pubmed]
  9. Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. Roberts, C.J., Nothwehr, S.F., Stevens, T.H. J. Cell Biol. (1992) [Pubmed]
  10. Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. Nothwehr, S.F., Roberts, C.J., Stevens, T.H. J. Cell Biol. (1993) [Pubmed]
  11. Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention. Bryant, N.J., Stevens, T.H. J. Cell Biol. (1997) [Pubmed]
  12. Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p. Voos, W., Stevens, T.H. J. Cell Biol. (1998) [Pubmed]
  13. Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane protein retention in Saccharomyces cerevisiae. Seeger, M., Payne, G.S. J. Cell Biol. (1992) [Pubmed]
  14. Allele-specific suppression of a defective trans-Golgi network (TGN) localization signal in Kex2p identifies three genes involved in localization of TGN transmembrane proteins. Redding, K., Brickner, J.H., Marschall, L.G., Nichols, J.W., Fuller, R.S. Mol. Cell. Biol. (1996) [Pubmed]
  15. Regulation of alpha-factor production in Saccharomyces cerevisiae: a-factor pheromone-induced expression of the MF alpha 1 and STE13 genes. Achstetter, T. Mol. Cell. Biol. (1989) [Pubmed]
 
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