Evidence map›Paper›PMID 27129777›Full record

ArticleThe Journal of biological chemistry2016

Ste24p Mediates Proteolysis of Both Isoprenylated and Non-prenylated Oligopeptides.

Emily R Hildebrandt, Buenafe T Arachea, Michael C Wiener, Walter K Schmidt

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.Acta crystallographica. Section D, Structural biology · 2018
    Article
  12. Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018
    Review
  13. Rce1: mechanism and inhibition.Critical reviews in biochemistry and molecular biology · 2018
    Review
  14. Article
  15. ZMPSTE24 defends against influenza and other pathogenic viruses.The Journal of experimental medicine · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. The impact of alterations in lamin A on genome integrity.Mutation research. Reviews in mutation research
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Emily R HildebrandtDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
Buenafe T AracheaDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908.
Michael C WienerDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908.
Walter K SchmidtDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602. Electronic address: wschmidt@bmb.uga.edu.
University of Georgia · USUniversity of Virginia · US

Funding

Structure and Function of the CaaX Protease Ste24pR01GM108612 · NIGMS · UNIVERSITY OF VIRGINIA · PI WIENER, MICHAEL · 2014 to 2017
$1.6M
Role of Proteolysis in Regulating CaaX Protein FunctionR01GM117148 · NIGMS · UNIVERSITY OF GEORGIA · PI SCHMIDT, WALTER K · 2016 to 2019
$1.2M
NIGMS NIH HHS R01 GM108612NIGMS NIH HHS R01 GM117148
6 · The paper itself

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 non-prenylated substrates, strongly suggestive of a role for substrate-membrane interaction in protease function. Mass spectroscopy analyses identify a cleavage preference at bonds where P1' is aliphatic in both isoprenylated and non-prenylated substrates, although this is not necessarily predictive. The identified cleavage sites are not at a fixed distance position relative to the C terminus. In this study, the substrates cleaved by Ste24p are based on known isoprenylated proteins (i.e. K-Ras4b and the yeast a-factor mating pheromone) and non-prenylated biological peptides (Aβ and insulin chains) that are known substrates of the M16A family of soluble zinc-dependent metalloproteases. These results establish that the substrate profile of Ste24p is broader than anticipated, being more similar to that of the M16A protease family than that of the Rce1p CAAX protease with which it has been functionally associated.

Indexed as

Membrane ProteinsMetalloendopeptidasesOligopeptidesProtein PrenylationProteolysisSaccharomyces cerevisiae ProteinsMembrane ProteinsMetalloendopeptidasesOligopeptidesSaccharomyces cerevisiae ProteinsSTE24 protein, S cerevisiaeenzyme kineticsmembrane enzymemetalloproteasepeptidaseprotein isoprenylation

Identifiers

PMID27129777
PMCPMC4933176
OpenAlexW2345277436

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.