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

• Neither rce1-null nor yor291w-null mutations affected PIO or the phenotype of spf1- or ste24-null mutants [4].

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].

References