Evidence map›Paper›PMID 26466678›Full record

ArticleMolecular biology of the cell2015

Phosphatidylserine translocation at the yeast trans-Golgi network regulates protein sorting into exocytic vesicles.

Hannah M Hankins, Yves Y Sere, Nicholas S Diab, Anant K Menon, Todd R Graham

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Lipid Transport byInfection and immunity · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
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.

Hannah M HankinsDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37235.
Yves Y SereDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065.
Nicholas S DiabDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37235.
Anant K MenonDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065.
Todd R GrahamDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37235 tr.graham@vanderbilt.edu.
Vanderbilt University · USCornell University · US

Funding

P4-ATPase mechanism of phospholipid translocationR01GM107978 · NIGMS · VANDERBILT UNIVERSITY · PI GRAHAM, TODD R · 2013 to 2021
$2.5M
NIGMS NIH HHS 1R01GM107978NIGMS NIH HHS R01 GM107978
6 · The paper itself

Abstract

Sorting of plasma membrane proteins into exocytic vesicles at the yeast trans-Golgi network (TGN) is believed to be mediated by their coalescence with specific lipids, but how these membrane-remodeling events are regulated is poorly understood. Here we show that the ATP-dependent phospholipid flippase Drs2 is required for efficient segregation of cargo into exocytic vesicles. The plasma membrane proteins Pma1 and Can1 are missorted from the TGN to the vacuole in drs2∆ cells. We also used a combination of flippase mutants that either gain or lose the ability to flip phosphatidylserine (PS) to determine that PS flip by Drs2 is its critical function in this sorting event. The primary role of PS flip at the TGN appears to be to control the oxysterol-binding protein homologue Kes1/Osh4 and regulate ergosterol subcellular distribution. Deletion of KES1 suppresses plasma membrane-missorting defects and the accumulation of intracellular ergosterol in drs2 mutants. We propose that PS flip is part of a homeostatic mechanism that controls sterol loading and lateral segregation of protein and lipid domains at the TGN.

Indexed as

Adenosine TriphosphatasesAmino Acid Transport Systems, BasicCalcium-Transporting ATPasesCell MembraneExocytosisMembrane ProteinsMutationOxysterol Binding ProteinsPhosphatidylserinesProtein TransportProton-Translocating ATPasesReceptors, SteroidSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinstrans-Golgi NetworkTransport VesiclesAdenosine TriphosphatasesAmino Acid Transport Systems, BasicCalcium-Transporting ATPasesCAN1 protein, S cerevisiaeDRS2 protein, S cerevisiaeKES1 protein, S cerevisiaeMembrane ProteinsOxysterol Binding ProteinsPhosphatidylserinesPMA1 protein, S cerevisiaeProton-Translocating ATPasesReceptors, SteroidSaccharomyces cerevisiae Proteins

Identifiers

PMID26466678
PMCPMC4678023
OpenAlexW2272816145

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.