Evidence map›Paper›PMID 22452743›Full record

ArticleBiochemistry2012

Allosteric activation of the phosphoinositide phosphatase Sac1 by anionic phospholipids.

Shurong Zhong, FoSheng Hsu, Christopher J Stefan, Xiaochun Wu, Anamika Patel, Michael S Cosgrove, Yuxin Mao

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  6. Review
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  8. Review
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  11. Lipid synthesis and transport are coupled to regulate membrane lipid dynamics in the endoplasmic reticulum.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  12. Article
  13. Article
  14. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  15. Review
  16. Article
  17. Lenz-Majewski mutations in PTDSS1 affect phosphatidylinositol 4-phosphate metabolism at ER-PM and ER-Golgi junctions.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Shurong ZhongWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, United States.
FoSheng Hsu
Christopher J Stefan
Xiaochun Wu
Anamika Patel
Michael S Cosgrove
Yuxin Mao
Cornell University · USSyracuse University · US

Funding

Molecular Mechanisms for the Assembly and Regulation of the MLL1 Core ComplexR01CA140522 · NCI · UPSTATE MEDICAL UNIVERSITY · PI COSGROVE, MICHAEL S. · 2010 to 2019
$3.6M
Structural and Functional Studies of the Sac Family Phosphoinositide PhosphatasesR01GM094347 · NIGMS · CORNELL UNIVERSITY · PI MAO, YUXIN · 2011 to 2015
$1.4M
NCI NIH HHS 1R01CA14052NCI NIH HHS R01 CA140522NIGMS NIH HHS 1R01GM094347
6 · The paper itself

Abstract

Sac family phosphoinositide phosphatases comprise an evolutionarily conserved family of enzymes in eukaryotes. Our recently determined crystal structure of the Sac phosphatase domain of yeast Sac1, the founding member of the Sac family proteins, revealed a unique conformation of the catalytic P-loop and a large positively charged groove at the catalytic site. We now report a unique mechanism for the regulation of its phosphatase activity. Sac1 is an allosteric enzyme that can be activated by its product phosphatidylinositol or anionic phospholipid phosphatidylserine. The activation of Sac1 may involve conformational changes of the catalytic P-loop induced by direct binding with the regulatory anionic phospholipids in the large cationic catalytic groove. These findings highlight the fact that lipid composition of the substrate membrane plays an important role in the control of Sac1 function.

Indexed as

Allosteric RegulationCatalytic DomainKineticsPhospholipidsPhosphoric Monoester HydrolasesProtein ConformationSaccharomyces cerevisiae ProteinsPhospholipidsPhosphoric Monoester HydrolasesSAC1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22452743
PMCPMC3329130
OpenAlexW2101141935

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.