Evidence map›Paper›PMID 28404745›Full record

ArticleMolecular biology of the cell2017

Quantitative high-content imaging identifies novel regulators of Neo1 trafficking at endosomes.

Lauren E Dalton, Björn D M Bean, Michael Davey, Elizabeth Conibear

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  8. Biallelic truncating variants inJournal of medical genetics · 2022
    Article
  9. Yeast as a Model to Find New Drugs and Drug Targets forInternational journal of molecular sciences · 2022
    Review
  10. Article
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  18. Conserved mechanism of phospholipid substrate recognition by the P4-ATPase Neo1 from Saccharomyces cerevisiae.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Article
  19. Review
  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

4 authors at 2 institutions in 1 country.

Lauren E DaltonCentre for Molecular Medicine and Therapeutics, BC Children's Hospital, University of British Columbia, Vancouver, BC V5Z 4H4, Canada.
Björn D M BeanCentre for Molecular Medicine and Therapeutics, BC Children's Hospital, University of British Columbia, Vancouver, BC V5Z 4H4, Canada.
Michael DaveyCentre for Molecular Medicine and Therapeutics, BC Children's Hospital, University of British Columbia, Vancouver, BC V5Z 4H4, Canada.
Elizabeth ConibearCentre for Molecular Medicine and Therapeutics, BC Children's Hospital, University of British Columbia, Vancouver, BC V5Z 4H4, Canada conibear@cmmt.ubc.ca.
BC Children's Hospital · CAUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P4-ATPases are a family of putative phospholipid flippases that regulate lipid membrane asymmetry, which is important for vesicle formation. Two yeast flippases, Drs2 and Neo1, have nonredundant functions in the recycling of the synaptobrevin-like v-SNARE Snc1 from early endosomes. Drs2 activity is needed to form vesicles and regulate its own trafficking, suggesting that flippase activity and localization are linked. However, the role of Neo1 in endosomal recycling is not well characterized. To identify novel regulators of Neo1 trafficking and activity at endosomes, we first identified mutants with impaired recycling of a Snc1-based reporter and subsequently used high-content microscopy to classify these mutants based on the localization of Neo1 or its binding partners, Mon2 and Dop1. This analysis identified a role for Arl1 in stabilizing the Mon2/Dop1 complex and uncovered a new function for Vps13 in early endosome recycling and Neo1 localization. We further showed that the cargo-selective sorting nexin Snx3 is required for Neo1 trafficking and identified an Snx3 sorting motif in the Neo1 N-terminus. Of importance, the Snx3-dependent sorting of Neo1 was required for the correct sorting of another Snx3 cargo protein, suggesting that the incorporation of Neo1 into recycling tubules may influence their formation.

Indexed as

Adenosine TriphosphatasesCarrier ProteinsEndosomesMembrane Transport ProteinsPhospholipid Transfer ProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsSorting NexinsTransport VesiclesVesicular Transport ProteinsAdenosine TriphosphatasesCarrier ProteinsMembrane Transport ProteinsNEO1 protein, S cerevisiaePhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsSNX3 protein, S cerevisiaeSorting NexinsVesicular Transport Proteins

Identifiers

PMID28404745
PMCPMC5449152
OpenAlexW2607472529

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.