Evidence map›Paper›PMID 23250744›Full record

ArticleThe Journal of biological chemistry2013

Phospholipid flippases Lem3p-Dnf1p and Lem3p-Dnf2p are involved in the sorting of the tryptophan permease Tat2p in yeast.

Takeru Hachiro, Takaharu Yamamoto, Kenji Nakano, Kazuma Tanaka

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. P-Type ATPase Apt1 of the Fungal PathogenJournal of fungi (Basel, Switzerland) · 2021
    Article
  5. Article
  6. Exomer complex regulates protein traffic at the TGN through differential interactions with cargos and clathrin adaptor complexes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  7. Lipid flippases in polarized growth.Current genetics · 2021
    Review
  8. Review
  9. Article
  10. Role of lipid transporters in fungal physiology and pathogenicity.Computational and structural biotechnology journal · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. P4-ATPases: lipid flippases in cell membranes.Pflugers Archiv : European journal of physiology · 2014
    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 1 institution in 1 country.

Takeru HachiroDivision of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Life Science, N15 W7, Kita-ku, Sapporo 060-0815, Japan.
Takaharu Yamamoto
Kenji Nakano
Kazuma Tanaka
Hokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type 4 P-type ATPases are flippases that generate phospholipid asymmetry in membranes. In budding yeast, heteromeric flippases, including Lem3p-Dnf1p and Lem3p-Dnf2p, translocate phospholipids to the cytoplasmic leaflet of membranes. Here, we report that Lem3p-Dnf1/2p are involved in transport of the tryptophan permease Tat2p to the plasma membrane. The lem3Δ mutant exhibited a tryptophan requirement due to the mislocalization of Tat2p to intracellular membranes. Tat2p was relocalized to the plasma membrane when trans-Golgi network (TGN)-to-endosome transport was inhibited. Inhibition of ubiquitination by mutations in ubiquitination machinery also rerouted Tat2p to the plasma membrane. Lem3p-Dnf1/2p are localized to endosomal/TGN membranes in addition to the plasma membrane. Endocytosis mutants, in which Lem3p-Dnf1/2p are sequestered to the plasma membrane, also exhibited the ubiquitination-dependent missorting of Tat2p. These results suggest that Tat2p is ubiquitinated at the TGN and missorted to the vacuolar pathway in the lem3Δ mutant. The NH(2)-terminal cytoplasmic region of Tat2p containing ubiquitination acceptor lysines interacted with liposomes containing acidic phospholipids, including phosphatidylserine. This interaction was abrogated by alanine substitution mutations in the basic amino acids downstream of the ubiquitination sites. Interestingly, a mutant Tat2p containing these substitutions was missorted in a ubiquitination-dependent manner. We propose the following model based on these results; Tat2p is not ubiquitinated when the NH(2)-terminal region is bound to membrane phospholipids, but if it dissociates from the membrane due to a low level of phosphatidylserine caused by perturbation of phospholipid asymmetry in the lem3Δ mutant, Tat2p is ubiquitinated and then transported from the TGN to the vacuole.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAmino Acid Transport SystemsATP-Binding Cassette TransportersCell MembraneEndocytosisMembrane Transport ProteinsMolecular Sequence DataMutationPhosphatidylserinesPhospholipid Transfer ProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinstrans-Golgi NetworkTryptophanAdenosine TriphosphatasesAmino Acid Transport SystemsATP-Binding Cassette TransportersDnf1 protein, S cerevisiaeDnf2 protein, S cerevisiaeLem3 protein, S cerevisiaeMembrane Transport ProteinsPhosphatidylserinesPhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsTAT2 protein, S cerevisiaeTryptophan

Identifiers

PMID23250744
PMCPMC3561578
OpenAlexW1971859508

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.