Evidence map›Paper›PMID 27203179›Full record

ArticleMolecular cell2016

Cyclin-Dependent Kinase Co-Ordinates Carbohydrate Metabolism and Cell Cycle in S. cerevisiae.

Gang Zhao, Yuping Chen, Lucas Carey, Bruce Futcher

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 83 citations in OpenAlex.

  1. Cln3 can work independently of Whi5 on the cell size for Start in yeast.bioRxiv : the preprint server for biology · 2025
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  7. The Yeast Ribosomal Protein Rpl1b Is Not Required for Respiration.International journal of molecular sciences · 2024
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  17. TheFrontiers in microbiology · 2022
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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

4 authors at 1 institution in 1 country.

Gang ZhaoDepartment of Molecular Genetics & Microbiology, Stony Brook University, Stony Brook, NY 11794, USA.
Yuping ChenDepartment of Molecular Genetics & Microbiology, Stony Brook University, Stony Brook, NY 11794, USA; Graduate Program in Genetics, Stony Brook University, Stony Brook, NY 11794, USA.
Lucas CareyDepartment of Molecular Genetics & Microbiology, Stony Brook University, Stony Brook, NY 11794, USA.
Bruce FutcherDepartment of Molecular Genetics & Microbiology, Stony Brook University, Stony Brook, NY 11794, USA. Electronic address: bfutcher@gmail.com.
Stony Brook University · US

Funding

SIZE CONTROL &COMMITMENT TO DIVISION IN S. CEREVISIAER01GM039978 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI FUTCHER, BRUCE BRUCE · 1988 to 2014
$4.3M
NIGMS NIH HHS R01 GM039978
6 · The paper itself

Abstract

Cyclin-dependent kinases (CDKs) control cell division in eukaryotes by phosphorylating proteins involved in division. But successful proliferation requires co-ordination between division and cellular growth in mass. Previous proteomic studies suggested that metabolic proteins, as well as cell division proteins, could potentially be substrates of cyclin-dependent kinases. Here we focus on two metabolic enzymes of the yeast S. cerevisiae, neutral trehalase (Nth1) and glycogen phosphorylase (Gph1), and show that their activities are likely directly controlled by CDK activity, thus allowing co-ordinate regulation of carbohydrate metabolism with cell division processes. In this case, co-ordinate regulation may optimize the decision to undertake a final cell division as nutrients are being exhausted. Co-regulation of cell division processes and metabolic processes by CDK activity may be a general phenomenon important for co-ordinating the cell cycle with growth.

Indexed as

Carbohydrate MetabolismCell CycleEnergy MetabolismCDC28 Protein Kinase, S cerevisiaeGenotypeGlycogenGlycogen PhosphorylaseMutationPhenotypeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTime FactorsTrehalaseTrehaloseCDC28 Protein Kinase, S cerevisiaeGlycogenGlycogen PhosphorylaseNTH1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTrehalaseTrehalose

Identifiers

PMID27203179
PMCPMC4905568
OpenAlexW2404660821

What OpenQuestion holds

Textmetadata
LicenceTDM
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.