Evidence map›Paper›PMID 24108357›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

SUMOylation regulates the SNF1 protein kinase.

Kobi J Simpson-Lavy, Mark Johnston

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 55 citations in OpenAlex.

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  20. SUMOylation represses SnRK1 signaling in Arabidopsis.The Plant journal : for cell and molecular biology · 2016
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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

2 authors at 2 institutions in 1 country.

Kobi J Simpson-LavyDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, CO 80045.
Mark Johnston
Columbia University · USUniversity of Colorado Denver · US

Funding

GLUCOSE SENSING AND SIGNALLING IN YEASTR01GM032540 · NIGMS · WASHINGTON UNIVERSITY · PI JOHNSTON, HENRY MARK · 1985 to 2017
$5.7M
NIGMS NIH HHS GM32540NIGMS NIH HHS R01 GM032540
6 · The paper itself

Abstract

The AMP-activated protein kinase (AMPK) is a major stress sensor of mammalian cells. AMPK's homolog in the yeast Saccharomyces cerevisiae, the SNF1 protein kinase, is a central regulator of carbon metabolism that inhibits the Snf3/Rgt2-Rgt1 glucose sensing pathway and activates genes involved in respiration. We present evidence that glucose induces modification of the Snf1 catalytic subunt of SNF1 with the small ubiquitin-like modifier protein SUMO, catalyzed by the SUMO (E3) ligase Mms21. Our results suggest that SUMOylation of Snf1 inhibits its function in two ways: by interaction of SUMO attached to lysine 549 with a SUMO-interacting sequence motif located near the active site of Snf1, and by targeting Snf1 for destruction via the Slx5-Slx8 (SUMO-directed) ubiquitin ligase. These findings reveal another way SNF1 function is regulated in response to carbon source.

Indexed as

GlucoseImmunoblottingMutationPhosphorylationProtein BindingProtein Serine-Threonine KinasesProtein StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSUMO-1 ProteinSumoylationGlucoseMms21 protein, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesSUMO-1 Proteinprotein kinase regulationprotein modificationsignal transduction

Identifiers

PMID24108357
PMCPMC3808588
OpenAlexW2156503672

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.