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Gene Review

STE24  -  Ste24p

Saccharomyces cerevisiae S288c

Synonyms: A-factor-converting enzyme, AFC1, CAAX prenyl protease 1, J2032, PIO2, ...
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High impact information on STE24

  • Deletion of both AFC1 and RCE1 resulted in the loss of proteolytic processing of prenylated proteins [1].
  • Identification of the a-factor biosynthetic intermediate that accumulates in the ste24 mutant revealed that STE24 is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification is complete [2].
  • The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities [3].
  • In vitro assays indicated that farnesylation was compromised or undetectable for 11 a-factor variants that produced no detectable halo in the wild-type AFC1 RCE1 strain [3].
  • The effects of ste24- and spf1-null mutations on invertase secretion are additive, cell generation time is increased 60%, and cells become sensitive to cold and to heat shock [4].

Biological context of STE24


Associations of STE24 with chemical compounds

  • Both Afc1p and Rce1p were able to proteolyze a-factor with A, V, L, I, C, or M at the a(1) position, V, L, I, C, or M at the a(2) position, or any amino acid at the X position that was acceptable for prenylation of the cysteine [3].

Other interactions of STE24

  • First, we show that AFRP is produced intracellularly and that mutants (ste24 and axl1) that cannot produce mature a-factor due to an N-terminal processing defect are nevertheless normal for AFRP production [5].


  1. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Boyartchuk, V.L., Ashby, M.N., Rine, J. Science (1997) [Pubmed]
  2. A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor. Fujimura-Kamada, K., Nouvet, F.J., Michaelis, S. J. Cell Biol. (1997) [Pubmed]
  3. The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities. Trueblood, C.E., Boyartchuk, V.L., Picologlou, E.A., Rozema, D., Poulter, C.D., Rine, J. Mol. Cell. Biol. (2000) [Pubmed]
  4. Yeast genes controlling responses to topogenic signals in a model transmembrane protein. Tipper, D.J., Harley, C.A. Mol. Biol. Cell (2002) [Pubmed]
  5. A novel a-factor-related peptide of Saccharomyces cerevisiae that exits the cell by a Ste6p-independent mechanism. Chen, P., Choi, J.D., Wang, R., Cotter, R.J., Michaelis, S. Mol. Biol. Cell (1997) [Pubmed]
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