Evidence map›Paper›PMID 27385829›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Dynamics and architecture of the NRBF2-containing phosphatidylinositol 3-kinase complex I of autophagy.

Lindsey N Young, Kelvin Cho, Rosalie Lawrence, Roberto Zoncu, James H Hurley

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 1 synthesis or guideline pooled it, 94 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025
    Review
  7. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  8. Article
  9. Article
  10. Physiological functions of ULK1/2.Journal of molecular biology · 2024
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Class III PI3K Biology.Current topics in microbiology and immunology · 2022
    Article
  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

5 authors at 2 institutions in 1 country.

Lindsey N YoungDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720;
Kelvin ChoDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720;
Rosalie LawrenceDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720;
Roberto ZoncuDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720;
James H HurleyDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 jimhurley@berkeley.edu.
University of California, Berkeley · USQB3 · US

Funding

TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI NOGALES, EVA · 1994 to 2018
$27.6M
ENGINEERING ORGANELLE FUNCTION TO REWIRE CANCER CELL METABOLISMDP2CA195761 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZONCU, ROBERTO · 2014 to 2014
$2.4M
The Autophagy Initiation ComplexesR01GM111730 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H · 2014 to 2021
$2.2M
NCI NIH HHS DP2 CA195761NIGMS NIH HHS P01 GM051487NIGMS NIH HHS R01 GM111730
6 · The paper itself

Abstract

The class III phosphatidylinositol 3-kinase complex I (PI3KC3-C1) is central to autophagy initiation. We previously reported the V-shaped architecture of the four-subunit version of PI3KC3-C1 consisting of VPS (vacuolar protein sorting) 34, VPS15, BECN1 (Beclin 1), and ATG (autophagy-related) 14. Here we show that a putative fifth subunit, nuclear receptor binding factor 2 (NRBF2), is a tightly bound component of the complex that profoundly affects its activity and architecture. NRBF2 enhances the lipid kinase activity of the catalytic subunit, VPS34, by roughly 10-fold. We used hydrogen-deuterium exchange coupled to mass spectrometry and negative-stain electron microscopy to map NRBF2 to the base of the V-shaped complex. NRBF2 interacts primarily with the N termini of ATG14 and BECN1. We show that NRBF2 is a homodimer and drives the dimerization of the larger PI3KC3-C1 complex, with implications for the higher-order organization of the preautophagosomal structure.

Indexed as

AutophagyAdaptor Proteins, Vesicular TransportAutophagy-Related ProteinsBeclin-1Class III Phosphatidylinositol 3-KinasesEscherichia coliHEK293 CellsHumansTrans-ActivatorsAdaptor Proteins, Vesicular TransportATG14 protein, humanAutophagy-Related ProteinsBeclin-1BECN1 protein, humanClass III Phosphatidylinositol 3-KinasesNRBF2 protein, humanTrans-Activatorsallosteryelectron microscopyhydrogen–deuterium exchange

Identifiers

PMID27385829
PMCPMC4961193
OpenAlexW2469694753

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.