Evidence map›Paper›PMID 18243114›Full record

ArticleMolecular cell2008

Functional anatomy of phospholipid binding and regulation of phosphoinositide homeostasis by proteins of the sec14 superfamily.

Gabriel Schaaf, Eric A Ortlund, Kimberly R Tyeryar, Carl J Mousley, Kristina E Ile, Teresa A Garrett, Jihui Ren, Melissa J Woolls, Christian R H Raetz, Matthew R Redinbo and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers.

0numbers the graph read from it
0cells of the map it votes in
144citing papers in PubMed
5.3field-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

144 citing papers in PubMed, 240 citations in OpenAlex.

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  16. Reconstitution of ORP-mediated lipid exchange coupled to PI4P metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  18. SF-1 Induces Nuclear PIP2.Biomolecules · 2023
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84 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Gabriel SchaafDepartment of Cell and Developmental Biology, School of Medicine, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7090, USA.
Eric A Ortlund
Kimberly R Tyeryar
Carl J Mousley
Kristina E Ile
Teresa A Garrett
Jihui Ren
Melissa J Woolls
Christian R H Raetz
Matthew R Redinbo
Vytas A Bankaitis
University of North Carolina at Chapel Hill · USDuke Medical Center · USDuke University Hospital · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
Tri-Institutional Molecular Mycology and Pathogenesis Training ProgramT32AI052080 · NIAID · DUKE UNIVERSITY · PI ANDREW ALSPAUGH, JOSEPH HEITMAN · 2003 to 2026
$8.7M
Role of the Phospholipids in Golgi Secretory FunctionR01GM044530 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BANKAITIS, VYTAS A · 1991 to 2019
$5.6M
Structure and Function of the Human Pregnane X ReceptorR01DK062229 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI REDINBO, MATTHEW · 2002 to 2006
$1.7M
NIAID NIH HHS 5T32 AI 052080NIAID NIH HHS T32 AI052080NIDDK NIH HHS DK 62229NIDDK NIH HHS R01 DK062229NIGMS NIH HHS GM 069338NIGMS NIH HHS GM 44530NIGMS NIH HHS R01 GM044530NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

Sec14, the major yeast phosphatidylinositol (PtdIns)/phosphatidylcholine (PtdCho) transfer protein, regulates essential interfaces between lipid metabolism and membrane trafficking from the trans-Golgi network (TGN). How Sec14 does so remains unclear. We report that Sec14 binds PtdIns and PtdCho at distinct (but overlapping) sites, and both PtdIns- and PtdCho-binding activities are essential Sec14 activities. We further show both activities must reside within the same molecule to reconstitute a functional Sec14 and for effective Sec14-mediated regulation of phosphoinositide homeostasis in vivo. This regulation is uncoupled from PtdIns-transfer activity and argues for an interfacial presentation mode for Sec14-mediated potentiation of PtdIns kinases. Such a regulatory role for Sec14 is a primary counter to action of the Kes1 sterol-binding protein that antagonizes PtdIns 4-OH kinase activity in vivo. Collectively, these findings outline functional mechanisms for the Sec14 superfamily and reveal additional layers of complexity for regulating phosphoinositide homeostasis in eukaryotes.

Indexed as

1-Phosphatidylinositol 4-KinaseBiological TransportCell MembraneGolgi ApparatusHomeostasisLipid MetabolismMembrane ProteinsOxysterol Binding ProteinsPhosphatidylcholinesPhosphatidylinositolsPhospholipid Transfer ProteinsProtein Structure, TertiaryReceptors, SteroidSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins1-Phosphatidylinositol 4-KinaseKES1 protein, S cerevisiaeMembrane ProteinsOxysterol Binding ProteinsPhosphatidylcholinesPhosphatidylinositolsPhospholipid Transfer ProteinsReceptors, SteroidSaccharomyces cerevisiae ProteinsSEC14 protein, S cerevisiae

Identifiers

PMID18243114
PMCPMC7808562
OpenAlexW2104256906

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.