Evidence map›Paper›PMID 36169638›Full record

ArticleThe Journal of cell biology2022

PI4P and BLOC-1 remodel endosomal membranes into tubules.

Riddhi Atul Jani, Aurélie Di Cicco, Tal Keren-Kaplan, Silvia Vale-Costa, Daniel Hamaoui, Ilse Hurbain, Feng-Ching Tsai, Mathilde Di Marco, Anne-Sophie Macé, Yueyao Zhu and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

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  5. BORC assemblies integrate BLOC-1 subunits to diversify endosomal trafficking functions.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

18 authors at 5 institutions in 3 countries.

Riddhi Atul JaniInstitut Curie, Université PSL, CNRS, UMR144, Structure and Membrane Compartments, Paris, France.ORCID 0000-0002-0068-2166
Aurélie Di Cicco *Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie Curie, Paris, France.
Tal Keren-Kaplan *Neurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD.ORCID 0000-0002-3842-4461
Silvia Vale-Costa *Cell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Oeiras, Portugal.ORCID 0000-0002-1005-2651
Daniel Hamaoui *Institut Pasteur, Université de Paris Cité, CNRS UMR3691, Cellular biology of microbial infection, Paris, France.
Ilse HurbainInstitut Curie, Université PSL, CNRS, UMR144, Structure and Membrane Compartments, Paris, France.ORCID 0000-0002-0097-7773
Feng-Ching TsaiInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie Curie, Paris, France.ORCID 0000-0002-6869-5254
Mathilde Di MarcoInstitut Curie, Université PSL, CNRS, UMR144, Structure and Membrane Compartments, Paris, France.ORCID 0000-0003-3004-9633
Anne-Sophie MacéInstitut Curie, Université PSL, CNRS, UMR144, Cell and Tissue Imaging Facility (PICT-IBiSA), Paris, France.
Yueyao ZhuDepartment of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia, Philadelphia, PA.ORCID 0000-0001-6358-4996
Maria João AmorimCell Biology of Viral Infection Lab, Instituto Gulbenkian de Ciência, Oeiras, Portugal.ORCID 0000-0002-4129-6659
Patricia BassereauInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie Curie, Paris, France.ORCID 0000-0002-8544-6778
Juan S BonifacinoNeurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD.ORCID 0000-0002-5673-6370
Agathe SubtilInstitut Pasteur, Université de Paris Cité, CNRS UMR3691, Cellular biology of microbial infection, Paris, France.ORCID 0000-0002-7481-4846
Michael S MarksDepartment of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia, Philadelphia, PA.ORCID 0000-0001-7435-7262
Daniel Lévy *Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie Curie, Paris, France.ORCID 0000-0002-8949-4072
Graça Raposo *Institut Curie, Université PSL, CNRS, UMR144, Structure and Membrane Compartments, Paris, France.ORCID 0000-0001-9590-1298
Cédric DelevoyeInstitut Curie, Université PSL, CNRS, UMR144, Structure and Membrane Compartments, Paris, France.ORCID 0000-0002-3835-6649
Centre National de la Recherche Scientifique · FRChildren's Hospital of Philadelphia · USNational Institutes of Health · USInstituto Gulbenkian de Ciência · PTUniversidade Católica Portuguesa · PT

Funding

Hermansky Pudlak Syndrome &melanosome formationR01EY015625 · NEI · UNIVERSITY OF PENNSYLVANIA · PI Michael S Marks · 2004 to 2026
$9.2M
Centre National de la Recherche ScientifiqueEuropean Research CouncilFrench National Research Infrastructure France-BioImaging ANR10-INBS-04Fundação para a Ciência e a TecnologiaHorizon 2020 101001521Institut CurieInstitut National de la Santé et de la Recherche MédicaleInstituto Gulbenkian de CiênciaLabex ANR-11-LABX-0038Ligue Contre le CancerNational Institute of Child Health and Human DevelopmentNEI NIH HHS R01 EY015625NIH HHS R01 EY015625
6 · The paper itself

Abstract

Intracellular trafficking is mediated by transport carriers that originate by membrane remodeling from donor organelles. Tubular carriers contribute to the flux of membrane lipids and proteins to acceptor organelles, but how lipids and proteins impose a tubular geometry on the carriers is incompletely understood. Using imaging approaches on cells and in vitro membrane systems, we show that phosphatidylinositol-4-phosphate (PI4P) and biogenesis of lysosome-related organelles complex 1 (BLOC-1) govern the formation, stability, and functions of recycling endosomal tubules. In vitro, BLOC-1 binds and tubulates negatively charged membranes, including those containing PI4P. In cells, endosomal PI4P production by type II PI4-kinases is needed to form and stabilize BLOC-1-dependent recycling endosomal tubules. Decreased PI4KIIs expression impairs the recycling of endosomal cargoes and the life cycles of intracellular pathogens such as Chlamydia bacteria and influenza virus that exploit the membrane dynamics of recycling endosomes. This study demonstrates how a phospholipid and a protein complex coordinate the remodeling of cellular membranes into functional tubules.

Indexed as

EndosomesIntracellular MembranesIntracellular Signaling Peptides and ProteinsPhosphatidylinositol PhosphatesCell MembraneLysosomesProtein TransportIntracellular Signaling Peptides and Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol Phosphates

Identifiers

PMID36169638
PMCPMC9524204
OpenAlexW4297461611

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.