Evidence map›Paper›PMID 34830359›Full record

ArticleInternational journal of molecular sciences2021

The Rpd3-Complex Regulates Expression of Multiple Cell Surface Recycling Factors in Yeast.

Konstantina Amoiradaki, Kate R Bunting, Katherine M Paine, Josephine E Ayre, Karen Hogg, Kamilla M E Laidlaw, Chris MacDonald

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

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Special Issue: Yeast Cell Signaling Pathways (Volume 1).International journal of molecular sciences · 2023
    Article
  4. Article
  5. 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

7 authors at 1 institution in 1 country.

Konstantina AmoiradakiYork Biomedical Research Institute, Department of Biology, University of York, York YO10 5DD, UK.ORCID 0000-0002-2129-1885
Kate R BuntingYork Biomedical Research Institute, Department of Biology, University of York, York YO10 5DD, UK.
Katherine M PaineYork Biomedical Research Institute, Department of Biology, University of York, York YO10 5DD, UK.ORCID 0000-0003-3017-4995
Josephine E AyreYork Biomedical Research Institute, Department of Biology, University of York, York YO10 5DD, UK.ORCID 0000-0002-2009-3553
Karen HoggImaging and Cytometry Laboratory, Bioscience Technology Facility, University of York, York YO10 5DD, UK.ORCID 0000-0001-7015-5102
Kamilla M E LaidlawYork Biomedical Research Institute, Department of Biology, University of York, York YO10 5DD, UK.ORCID 0000-0001-9209-4806
Chris MacDonaldYork Biomedical Research Institute, Department of Biology, University of York, York YO10 5DD, UK.
University of York · GB

Funding

Wellcome Trust 204636/Z/16/Z
6 · The paper itself

Abstract

Intracellular trafficking pathways control residency and bioactivity of integral membrane proteins at the cell surface. Upon internalisation, surface cargo proteins can be delivered back to the plasma membrane via endosomal recycling pathways. Recycling is thought to be controlled at the metabolic and transcriptional level, but such mechanisms are not fully understood. In yeast, recycling of surface proteins can be triggered by cargo deubiquitination and a series of molecular factors have been implicated in this trafficking. In this study, we follow up on the observation that many subunits of the Rpd3 lysine deacetylase complex are required for recycling. We validate ten Rpd3-complex subunits in recycling using two distinct assays and developed tools to quantify both. Fluorescently labelled Rpd3 localises to the nucleus and complements recycling defects, which we hypothesised were mediated by modulated expression of Rpd3 target gene(s). Bioinformatics implicated 32 candidates that function downstream of Rpd3, which were over-expressed and assessed for capacity to suppress recycling defects of

Indexed as

1-Phosphatidylinositol 4-KinaseCell MembraneChromosomal Proteins, Non-HistoneEndosomesGene Expression Regulation, FungalHistone DeacetylasesHydroxymethyl and Formyl TransferasesMultiprotein ComplexesProtein Interaction MapsProtein Phosphatase 2Saccharomyces cerevisiaeSaccharomyces cerevisiae Proteins1-Phosphatidylinositol 4-KinaseChromosomal Proteins, Non-HistoneDIT1 protein, S cerevisiaeHistone DeacetylasesHydroxymethyl and Formyl TransferasesLDB7 protein, S cerevisiaeMultiprotein ComplexesPIK1 protein, S cerevisiaeProtein Phosphatase 2RPD3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSIT4 protein, S cerevisiaeendocytosishistone deacetylasemembrane traffickingsurface membrane proteinstranscription

Identifiers

PMID34830359
PMCPMC8617818
OpenAlexW3214770116

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.