2016
DOI: 10.1074/jbc.m116.718197
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Ste24p Mediates Proteolysis of Both Isoprenylated and Non-prenylated Oligopeptides

Abstract: Rce1p and Ste24p are integral membrane proteins involved in the proteolytic maturation of isoprenylated proteins. Extensive published evidence indicates that Rce1p requires the isoprenyl moiety as an important substrate determinant. By contrast, we report that Ste24p can cleave both isoprenylated and non-prenylated substrates in vitro, indicating that the isoprenyl moiety is not required for substrate recognition. Steady-state enzyme kinetics are significantly different for prenylated versus nonprenylated subs… Show more

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Cited by 24 publications
(40 citation statements)
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“…Proteolytic activity of yeast membranes containing overexpressed ZMPSTE24Δcys (cysteine-free human Ste24p, with the five nonconserved cysteines mutated to serine) was characterized with a modified version of existing IQF assays previously utilized for several yeast orthologs of Ste24p [23, 30]. The peptide substrate utilized, Abz-KSKTKC(farnesyl)VIK-Dnp, is cleaved by ZMPSTE24 to yield Abz-KSKTKC(farnesyl) and VIK-Dnp products [23].…”
Section: Resultsmentioning
confidence: 99%
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“…Proteolytic activity of yeast membranes containing overexpressed ZMPSTE24Δcys (cysteine-free human Ste24p, with the five nonconserved cysteines mutated to serine) was characterized with a modified version of existing IQF assays previously utilized for several yeast orthologs of Ste24p [23, 30]. The peptide substrate utilized, Abz-KSKTKC(farnesyl)VIK-Dnp, is cleaved by ZMPSTE24 to yield Abz-KSKTKC(farnesyl) and VIK-Dnp products [23].…”
Section: Resultsmentioning
confidence: 99%
“…The peptide substrate utilized, Abz-KSKTKC(farnesyl)VIK-Dnp, is cleaved by ZMPSTE24 to yield Abz-KSKTKC(farnesyl) and VIK-Dnp products [23]. To determine the membrane concentration to be used for the assay, a series of two-fold dilutions of ZMPSTE24Δcys enriched membranes were examined in the presence of 1, 10 and 40 μM of Abz-KSKTKC(farnesyl)VIK-Dnp.…”
Section: Resultsmentioning
confidence: 99%
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“…A recent report now shows that Ste24, a yeast homolog of ZMPSTE24, could cleave both prenylated and nonprenylated substrates, further indicating a much broader substrate profile for Ste24 and possibly ZMPSTE24. From this perspective, our unbiased proteomic study provides additional protein substrates for further studies (Hildebrandt et al 2016)…”
Section: Discussionmentioning
confidence: 99%