Evidence map›Paper›PMID 36169099›Full record

ArticleCell biochemistry and function2022

The phospholipid flippase ATP8B1 is required for lysosomal fusion in macrophages.

Valentina E Gómez-Mellado, Kam S Ho-Mok, Vincent A van der Mark, Nicole N van der Wel, Anita E Grootemaat, Arthur J Verhoeven, Ronald P J Oude Elferink, Coen C Paulusma

Open access · hybridAbstract read
In one paragraph

Article in Cell biochemistry and function, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 2 institutions in 1 country.

Valentina E Gómez-MelladoTytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology and Metabolism, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.ORCID http://orcid.org/0000-0003-4879-7795
Kam S Ho-MokTytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology and Metabolism, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.
Vincent A van der MarkTytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology and Metabolism, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.
Nicole N van der WelDepartment of Medical Biology, Electron Microscopy Center Amsterdam, Amsterdam University Medical Center, Amsterdam, The Netherlands.
Anita E GrootemaatDepartment of Medical Biology, Electron Microscopy Center Amsterdam, Amsterdam University Medical Center, Amsterdam, The Netherlands.
Arthur J VerhoevenTytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology and Metabolism, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.
Ronald P J Oude ElferinkTytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology and Metabolism, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.
Coen C PaulusmaTytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology and Metabolism, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.
Amsterdam University Medical Centers · NLAmsterdam UMC Location University of Amsterdam · NL

Funding

Tytgat Institute Grant
6 · The paper itself

Abstract

ATP8B1 is a phospholipid flippase and member of the type 4 subfamily of P-type ATPases (P4-ATPase) subfamily. P4-ATPases catalyze the translocation of phospholipids across biological membranes, ensuring proper membrane asymmetry, which is crucial for membrane protein targeting and activity, vesicle biogenesis, and barrier function. Here we have investigated the role of ATP8B1 in the endolysosomal pathway in macrophages. Depletion of ATP8B1 led to delayed degradation of content in the phagocytic pathway and in overacidification of the endolysosomal system. Furthermore, ATP8B1 knockdown cells exhibited large multivesicular bodies filled with intraluminal vesicles. Similar phenotypes were observed in CRISPR-generated ATP8B1 knockout cells. Importantly, induction of autophagy led to accumulation of autophagosomes in ATP8B1 knockdown cells. Collectively, our results support a novel role for ATP8B1 in lysosomal fusion in macrophages, a process crucial in the terminal phase of endolysosomal degradation.

Indexed as

Adenosine TriphosphatasesPhospholipidsCell MembraneLysosomesMembrane ProteinsAdenosine TriphosphatasesMembrane ProteinsPhospholipidsATP8B1CDC50Aflippaselate endosomeslysosomal fusionmultivesicular bodiesPFIC1phospholipid

Identifiers

PMID36169099
PMCPMC10087937
OpenAlexW4297457205

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.