Evidence map›Paper›PMID 22933563›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2012

Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.

Susan Michaelis, Jemima Barrowman

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

64 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A yeast mating platform for multiplex screening of fungal GPCR-ligand interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Molecular Response ofJournal of fungi (Basel, Switzerland) · 2023
    Article
  10. Article
  11. Pheromone Response and Mating Behavior in Fission Yeast.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  12. Mechanism of commitment to a mating partner inMolecular biology of the cell · 2022
    Article
  13. Article
  14. Article
  15. Peptidome: Chaos or Inevitability.International journal of molecular sciences · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Through the back door: Unconventional protein secretion.Cell surface (Amsterdam, Netherlands) · 2020
    Review
  20. Review

4 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

2 authors at 1 institution in 1 country.

Susan MichaelisDepartment of Cell Biology, The Johns Hopkins School of Medicine, Baltimore, Maryland, USA. michaelis@jhmi.edu
Jemima Barrowman
Johns 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
Trafficking of ABC proteins in yeastR01GM051508 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MICHAELIS, SUSAN D. · 1994 to 2010
$3.3M
NIGMS NIH HHS GM41223NIGMS NIH HHS GM51508NIGMS NIH HHS R01 GM041223NIGMS NIH HHS R01 GM051508
6 · The paper itself

Abstract

The mating pheromone a-factor secreted by Saccharomyces cerevisiae is a farnesylated and carboxylmethylated peptide and is unusually hydrophobic compared to other extracellular signaling molecules. Mature a-factor is derived from a precursor with a C-terminal CAAX motif that directs a series of posttranslational reactions, including prenylation, endoproteolysis, and carboxylmethylation. Historically, a-factor has served as a valuable model for the discovery and functional analysis of CAAX-processing enzymes. In this review, we discuss the three modules comprising the a-factor biogenesis pathway: (i) the C-terminal CAAX-processing steps carried out by Ram1/Ram2, Ste24 or Rce1, and Ste14; (ii) two sequential N-terminal cleavage steps, mediated by Ste24 and Axl1; and (iii) export by a nonclassical mechanism, mediated by the ATP binding cassette (ABC) transporter Ste6. The small size and hydrophobicity of a-factor present both challenges and advantages for biochemical analysis, as discussed here. The enzymes involved in a-factor biogenesis are conserved from yeasts to mammals. Notably, studies of the zinc metalloprotease Ste24 in S. cerevisiae led to the discovery of its mammalian homolog ZMPSTE24, which cleaves the prenylated C-terminal tail of the nuclear scaffold protein lamin A. Mutations that alter ZMPSTE24 processing of lamin A in humans cause the premature-aging disease progeria and related progeroid disorders. Intriguingly, recent evidence suggests that the entire a-factor pathway, including all three biogenesis modules, may be used to produce a prenylated, secreted signaling molecule involved in germ cell migration in Drosophila. Thus, additional prenylated signaling molecules resembling a-factor, with as-yet-unknown roles in metazoan biology, may await discovery.

Indexed as

AnimalsDrosophilaHumansMating FactorPeptidesProgeriaSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionMating FactorPeptidesSaccharomyces cerevisiae Proteins

Identifiers

PMID22933563
PMCPMC3429625
OpenAlexW2123943386

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.