Evidence map›Paper›PMID 9736709›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage.

W K Schmidt, A Tam, K Fujimura-Kamada, S Michaelis

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

82 citing papers in PubMed, 186 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Post-translational modification of RAS proteins.Current opinion in structural biology · 2021
    Review
  11. Review
  12. Article
  13. Interaction between RAS gene and lipid metabolism in cancer.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Posttranslational Modifications of RAS Proteins.Cold Spring Harbor perspectives in medicine · 2018
    Review

22 more citing papers are in PubMed but not listed here.

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 2 countries.

W K SchmidtDepartment of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
A Tam
K Fujimura-Kamada
S Michaelis
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

The integral membrane protease ZMPSTE24, lamin A processing, and progeriaR01GM041223 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MICHAELIS, SUSAN D. · 1989 to 2017
$5.0M
CAAX PROCESSING PATHWAY COMPONENTSF32GM018641 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHMIDT, WALTER K · 1997 to 1998
–
NIGMS NIH HHS F32 GM018641NIGMS NIH HHS GM18641NIGMS NIH HHS GM41223NIGMS NIH HHS R01 GM041223
6 · The paper itself

Abstract

Proteins terminating in the CAAX motif, for example Ras and the yeast a-factor mating pheromone, are prenylated, trimmed of their last three amino acids, and carboxyl-methylated. The enzymes that mediate these activities, collectively referred to as CAAX processing components, have been identified genetically in Saccharomyces cerevisiae. Whereas the Ram1p/Ram2p prenyltransferase is a cytosolic soluble enzyme, sequence analysis predicts that the other CAAX processing components, the Rce1p and Ste24p proteases and the Ste14p methyltransferase, contain multiple membrane spans. To determine the intracellular site(s) at which CAAX processing occurs, we have examined the localization of the CAAX proteases Rce1p and Ste24p by subcellular fractionation and indirect immunofluorescence. We find that both of these proteases are associated with the endoplasmic reticulum (ER) membrane. In addition to having a role in CAAX processing, the Ste24p protease catalyzes the first of two cleavage steps that remove the amino-terminal extension from the a-factor precursor, suggesting that the first amino-terminal processing step of a-factor maturation also occurs at the ER membrane. The ER localization of Ste24p is consistent with the presence of a carboxyl-terminal dilysine ER retrieval motif, although we find that mutation of this motif does not result in mislocalization of Ste24p. Because the ER is not the ultimate destination for a-factor or most CAAX proteins, our results imply that a mechanism must exist for the intracellular routing of CAAX proteins from the ER membrane to other cellular sites.

Indexed as

Saccharomyces cerevisiae ProteinsCell FractionationEndopeptidasesEndoplasmic ReticulumFluorescent Antibody TechniqueFungal ProteinsGenetic Complementation TestMembrane ProteinsMetalloendopeptidasesProprotein ConvertasesProtein Processing, Post-TranslationalSaccharomyces cerevisiaeEndopeptidasesFungal ProteinsMembrane ProteinsMetalloendopeptidasesProprotein ConvertasesRCE1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSTE24 protein, S cerevisiae

Identifiers

PMID9736709
PMCPMC21615
OpenAlexW2015763826

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.