Evidence map›Paper›PMID 25666509›Full record

ArticleMolecular and cellular biology2015

Role of the unfolded protein response in regulating the mucin-dependent filamentous-growth mitogen-activated protein kinase pathway.

Hema Adhikari, Nadia Vadaie, Jacky Chow, Lauren M Caccamise, Colin A Chavel, Boyang Li, Alexander Bowitch, Christopher J Stefan, Paul J Cullen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 43 citations in OpenAlex.

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  19. Spatial landmarks regulate a Cdc42-dependent MAPK pathway to control differentiation and the response to positional compromise.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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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

9 authors at 2 institutions in 1 country.

Hema AdhikariDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA.
Nadia VadaieDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA.
Jacky ChowDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA.
Lauren M CaccamiseDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA.
Colin A ChavelDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA.
Boyang LiDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA.
Alexander BowitchDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA.
Christopher J StefanWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York, USA.
Paul J CullenDepartment of Biological Sciences at SUNY-Buffalo, Buffalo, New York, USA pjcullen@buffalo.edu.
University at Buffalo, State University of New York · USCornell University · US

Funding

Control of MAPK Signaling by Cell Polarity ProteinsR01GM098629 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI CULLEN, PAUL JAMES · 2011 to 2024
$4.4M
Medical Research Council MC_UU_12018/6NIGMS NIH HHS GM098629NIGMS NIH HHS R01 GM098629
6 · The paper itself

Abstract

Signaling mucins are evolutionarily conserved regulators of signal transduction pathways. The signaling mucin Msb2p regulates the Cdc42p-dependent mitogen-activated protein kinase (MAPK) pathway that controls filamentous growth in yeast. The cleavage and release of the glycosylated inhibitory domain of Msb2p is required for MAPK activation. We show here that proteolytic processing of Msb2p was induced by underglycosylation of its extracellular domain. Cleavage of underglycosylated Msb2p required the unfolded protein response (UPR), a quality control (QC) pathway that operates in the endoplasmic reticulum (ER). The UPR regulator Ire1p, which detects misfolded/underglycosylated proteins in the ER, controlled Msb2p cleavage by regulating transcriptional induction of Yps1p, the major protease that processes Msb2p. Accordingly, the UPR was required for differentiation to the filamentous cell type. Cleavage of Msb2p occurred in conditional trafficking mutants that trap secretory cargo in the endomembrane system. Processed Msb2p was delivered to the plasma membrane, and its turnover by the ubiquitin ligase Rsp5p and ESCRT attenuated the filamentous-growth pathway. We speculate that the QC pathways broadly regulate signaling glycoproteins and their cognate pathways by recognizing altered glycosylation patterns that can occur in response to extrinsic cues.

Indexed as

MAP Kinase Signaling SystemUnfolded Protein ResponseGlycosylationIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein KinasesMucinsProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein KinasesMSB2 protein, S cerevisiaeMucinsSaccharomyces cerevisiae Proteins

Identifiers

PMID25666509
PMCPMC4372694
OpenAlexW2327409977

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.