Evidence map›Paper›PMID 18591427›Full record

ArticleThe Journal of cell biology2008

Cleavage of the signaling mucin Msb2 by the aspartyl protease Yps1 is required for MAPK activation in yeast.

Nadia Vadaie, Heather Dionne, Darowan S Akajagbor, Seth R Nickerson, Damian J Krysan, Paul J Cullen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

76 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. The GPI-Anchored Aspartyl Proteases Encoded by theJournal of fungi (Basel, Switzerland) · 2025
    Article
  3. Article
  4. Role ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Mucins and the Microbiome.Annual review of biochemistry · 2020
    Review
  18. Article
  19. Article
  20. Article

16 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

6 authors at 2 institutions in 1 country.

Nadia VadaieDepartment of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA.
Heather Dionne
Darowan S Akajagbor
Seth R Nickerson
Damian J Krysan
Paul J Cullen
University at Buffalo, State University of New York · USUniversity of Rochester Medical Center · US

Funding

Yeast Aspartyl Proteases in Cell Wall IntegrityK08AI062978 · NIAID · UNIVERSITY OF ROCHESTER · PI KRYSAN, DAMIAN J · 2005 to 2007
$367k
A Model Signaling Mucin in YeastR03DE018425 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI CULLEN, PAUL JAMES · 2007 to 2008
$158k
NIAID NIH HHS K08 AI062978NIAID NIH HHS K08AI062978NIDCR NIH HHS 1R03DE018425-01NIDCR NIH HHS R03 DE018425NIGMS NIH HHS GM 0535393T
6 · The paper itself

Abstract

Signaling mucins are cell adhesion molecules that activate RAS/RHO guanosine triphosphatases and their effector mitogen-activated protein kinase (MAPK) pathways. We found that the Saccharomyces cerevisiae mucin Msb2p, which functions at the head of the Cdc42p-dependent MAPK pathway that controls filamentous growth, is processed into secreted and cell-associated forms. Cleavage of the extracellular inhibitory domain of Msb2p by the aspartyl protease Yps1p generated the active form of the protein by a mechanism incorporating cellular nutritional status. Activated Msb2p functioned through the tetraspan protein Sho1p to induce MAPK activation as well as cell polarization, which involved the Cdc42p guanine nucleotide exchange factor Cdc24p. We postulate that cleavage-dependent activation is a general feature of signaling mucins, which brings to light a novel regulatory aspect of this class of signaling adhesion molecule.

Indexed as

Signal TransductionAspartic Acid EndopeptidasesEnzyme ActivationEnzyme InductionGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsMAP Kinase Signaling SystemMitogen-Activated Protein KinasesMucinsPeptidesProtein BindingProtein Processing, Post-TranslationalProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAspartic Acid EndopeptidasesGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein KinasesMSB2 protein, S cerevisiaeMucinsPeptidesSaccharomyces cerevisiae ProteinsYPS1 protein, S cerevisiae

Identifiers

PMID18591427
PMCPMC2442203
OpenAlexW2112986374

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.