Evidence map›Paper›PMID 37114947›Full record

ArticleMolecular and cellular biology2023

Chaperone-Dependent Degradation of Cdc42 Promotes Cell Polarity and Shields the Protein from Aggregation.

Beatriz González, Martí Aldea, Paul J Cullen

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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

3 authors at 2 institutions in 2 countries.

Beatriz GonzálezDepartment of Biological Sciences, State University of New York at Buffalo, New York, USA.
Martí AldeaMolecular Biology Institute of Barcelona (IBMB), CSIC, Barcelona, Spain.
Paul J CullenDepartment of Biological Sciences, State University of New York at Buffalo, New York, USA.
University at Buffalo, State University of New York · USInstitut de Biologia Molecular de Barcelona · ES

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
NIGMS NIH HHS R01 GM098629
6 · The paper itself

Abstract

Rho GTPases are global regulators of cell polarity and signaling. By exploring the turnover regulation of the yeast Rho GTPase Cdc42p, we identified new regulatory features surrounding the stability of the protein. We specifically show that Cdc42p is degraded at 37 °C by chaperones through lysine residues located in the C-terminus of the protein. Cdc42p turnover at 37 °C occurred by the 26S proteasome in an ESCRT-dependent manner in the lysosome/vacuole. By analyzing versions of Cdc42p that were defective for turnover, we show that turnover at 37 °C promoted cell polarity but was defective for sensitivity to mating pheromone, presumably mediated through a Cdc42p-dependent MAP kinase pathway. We also identified one residue (K16) in the P-loop of the protein that was critical for Cdc42p stability. Accumulation of Cdc42p

Indexed as

cdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell PolaritySaccharomyces cerevisiae ProteinsHumansSaccharomyces cerevisiaeSignal Transductioncdc42 GTP-Binding Protein, Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsagingESCRTprotein aggregationprotein traffickingquality controlsexual selectiontemperaturetradeoffs

Identifiers

PMID37114947
PMCPMC10184603
OpenAlexW4367312857

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.