Evidence map›Paper›PMID 30659099›Full record

ArticleThe Journal of cell biology2019

The activity of Sac1 across ER-TGN contact sites requires the four-phosphate-adaptor-protein-1.

Rossella Venditti, Maria Chiara Masone, Laura Rita Rega, Giuseppe Di Tullio, Michele Santoro, Elena Polishchuk, Ivan Castello Serrano, Vesa M Olkkonen, Akihiro Harada, Diego L Medina and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
6.7field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 87 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Molecular mechanisms of polarized transport to the apical plasma membrane.Frontiers in cell and developmental biology · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Phosphoinositide transport and metabolism at membrane contact sites.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2022
    Review
  17. Article
  18. Review
  19. Intracellular Cholesterol Synthesis and Transport.Frontiers in cell and developmental biology · 2022
    Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 3 countries.

Rossella VendittiTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Maria Chiara MasoneTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Laura Rita RegaTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Giuseppe Di TullioTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Michele SantoroTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Elena PolishchukTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Ivan Castello SerranoTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Vesa M OlkkonenMinerva Foundation Institute for Medical Research, Biomedicum 2U, Helsinki, Finland.
Akihiro HaradaOsaka University, Osaka, Japan.ORCID 0000-0002-2484-9784
Diego L MedinaTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.ORCID 0000-0002-7347-2645
Raffaele La MontagnaTelethon Institute of Genetics and Medicine, Pozzuoli, Italy.
Maria Antonietta De MatteisTelethon Institute of Genetics and Medicine, Pozzuoli, Italy dematteis@tigem.it.ORCID 0000-0003-0053-3061
Telethon Institute Of Genetics And Medicine · ITThe University of Osaka · JPUniversity of Helsinki · FI

Funding

European Research Council 670881Telethon TGM11CB1
6 · The paper itself

Abstract

Phosphatidylinositol-4-phosphate (PI4P), a phosphoinositide with key roles in the Golgi complex, is made by Golgi-associated phosphatidylinositol-4 kinases and consumed by the 4-phosphatase Sac1 that, instead, is an ER membrane protein. Here, we show that the contact sites between the ER and the TGN (ERTGoCS) provide a spatial setting suitable for Sac1 to dephosphorylate PI4P at the TGN. The ERTGoCS, though necessary, are not sufficient for the phosphatase activity of Sac1 on TGN PI4P, since this needs the phosphatidyl-four-phosphate-adaptor-protein-1 (FAPP1). FAPP1 localizes at ERTGoCS, interacts with Sac1, and promotes its in-trans phosphatase activity in vitro. We envision that FAPP1, acting as a PI4P detector and adaptor, positions Sac1 close to TGN domains with elevated PI4P concentrations allowing PI4P consumption. Indeed, FAPP1 depletion induces an increase in TGN PI4P that leads to increased secretion of selected cargoes (e.g., ApoB100), indicating that FAPP1, by controlling PI4P levels, acts as a gatekeeper of Golgi exit.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsEndoplasmic ReticulumGolgi ApparatusHeLa CellsHep G2 CellsHumansMembrane ProteinsMicePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesAdaptor Proteins, Signal TransducingMembrane Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesPLEKHA3 protein, humanSACM1L protein, human

Identifiers

PMID30659099
PMCPMC6400556
OpenAlexW2909563142

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.