Evidence map›Paper›PMID 22025676›Full record

ArticleMolecular and cellular biology2012

Desumoylation of the endoplasmic reticulum membrane VAP family protein Scs2 by Ulp1 and SUMO regulation of the inositol synthesis pathway.

Rachael Felberbaum, Nicole R Wilson, Dongmei Cheng, Junmin Peng, Mark Hochstrasser

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

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  11. Review
  12. Function and regulation of SUMO proteases.Nature reviews. Molecular cell biology · 2012
    Review
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

5 authors at 2 institutions in 1 country.

Rachael FelberbaumDepartments of Molecular, Cell, & Developmental Biology, Yale University, New Haven, Connecticut, USA.
Nicole R Wilson
Dongmei Cheng
Junmin Peng
Mark Hochstrasser
Yale University · USEmory University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
FUNCTIONS AND MECHANISMS OF DEUBIQUITINATING ENZYMESR01GM053756 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1996 to 2019
$6.5M
SUMO Regulation of mRNA SurveillanceF31AG032166 · NIA · YALE UNIVERSITY · PI FELBERBAUM, RACHAEL S. · 2008 to 2009
$60k
NIA NIH HHS F31 AG032166NIA NIH HHS F31-AG032166NIGMS NIH HHS GM053756NIGMS NIH HHS R01 GM053756NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32-GM007223
6 · The paper itself

Abstract

Posttranslational protein modification by the ubiquitin-like SUMO protein is critical to eukaryotic cell regulation, but much remains unknown regarding its operation and substrates. Here we report that specific mutations in the Saccharomyces cerevisiae Ulp1 SUMO protease, including its coiled-coil (CC) domain, lead to the accumulation of distinct sumoylated proteins in vivo. A prominent ~50-kDa sumoylated protein accumulates in a Ulp1 CC mutant. The protein was identified as Scs2, an endoplasmic reticulum (ER) membrane protein that regulates phosphatidylinositol synthesis and lipid trafficking. Mutation of lysine 180 of Scs2 abolishes its sumoylation. Notably, impairment of either cellular sumoylation or cellular desumoylation mechanisms inhibits cell growth in the absence of inositol and exacerbates the inositol auxotrophy caused by deletion of SCS2. Mutants lacking the Ulp2 SUMO protease are the most severely affected, and this defect was traced to the mutants' impaired ability to induce transcription of INO1, which encodes the rate-limiting enzyme of inositol biosynthesis. Conversely, inositol starvation induces a striking change in the profiles of total cellular SUMO conjugates. These results provide the first evidence of cross-regulation between the SUMO and inositol pathways, including the sumoylation of an ER membrane protein central to phospholipid synthesis and phosphoinositide signaling.

Indexed as

SumoylationCysteine EndopeptidasesEndopeptidasesGene Expression Regulation, FungalInositolMembrane ProteinsMutationMyo-Inositol-1-Phosphate SynthaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsTranscriptional ActivationCysteine EndopeptidasesEndopeptidasesINO1 protein, S cerevisiaeInositolMembrane ProteinsMyo-Inositol-1-Phosphate SynthaseSaccharomyces cerevisiae ProteinsScs2 protein, S cerevisiaeSmall Ubiquitin-Related Modifier ProteinsSMT3 protein, S cerevisiaeUlp1 proteaseULP2 protein, S cerevisiae

Identifiers

PMID22025676
PMCPMC3255706
OpenAlexW2155883550

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.