Evidence map›Paper›PMID 31464684›Full record

ArticleeLife2019

A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex.

Edward A Partlow, Richard W Baker, Gwendolyn M Beacham, Joshua S Chappie, Andres E Leschziner, Gunther Hollopeter

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Article
  7. A structure-based mechanism for initiation of AP-3 coated vesicle formation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. eLife · 2024
    Article
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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

6 authors at 2 institutions in 1 country.

Edward A Partlow *Department of Molecular Medicine, Cornell University, New York, United States.ORCID 0000-0001-5513-088X
Richard W Baker *Department of Cellular and Molecular Medicine, School of Medicine, University of California, San Diego, La Jolla, United States.ORCID 0000-0003-1136-6000
Gwendolyn M BeachamDepartment of Molecular Medicine, Cornell University, New York, United States.ORCID 0000-0001-7158-6887
Joshua S ChappieDepartment of Molecular Medicine, Cornell University, New York, United States.ORCID 0000-0002-5733-7275
Andres E LeschzinerDepartment of Cellular and Molecular Medicine, School of Medicine, University of California, San Diego, La Jolla, United States.
Gunther HollopeterDepartment of Molecular Medicine, Cornell University, New York, United States.ORCID 0000-0002-6409-0530
Cornell University · USUniversity of California San Diego · US

Funding

Molecular regulation of the AP2 clathrin adaptor complexR01GM127548 · NIGMS · CORNELL UNIVERSITY · PI HOLLOPETER, GUNTHER · 2019 to 2023
$2.1M
Broad wavelength range Zeiss 780 NLO/confocal system for the Cornell Imaging CoreS10OD018516 · OD · CORNELL UNIVERSITY · PI ZIPFEL, WARREN R · 2014 to 2014
$834k
Damon Runyon Cancer Research Foundation DRG-#2285-17NIGMS NIH HHS R01 GM127548NIGMS NIH HHS R01 GM127548-01A1NIH HHS S10 OD018516
6 · The paper itself

Abstract

Endocytosis of transmembrane proteins is orchestrated by the AP2 clathrin adaptor complex. AP2 dwells in a closed, inactive state in the cytosol, but adopts an open, active conformation on the plasma membrane. Membrane-activated complexes are also phosphorylated, but the significance of this mark is debated. We recently proposed that NECAP negatively regulates AP2 by binding open and phosphorylated complexes (Beacham et al., 2018). Here, we report high-resolution cryo-EM structures of NECAP bound to phosphorylated AP2. The site of AP2 phosphorylation is directly coordinated by residues of the NECAP PHear domain that are predicted from genetic screens in

Indexed as

Protein Processing, Post-TranslationalAdaptor Protein Complex 2Adaptor Proteins, Vesicular TransportCaenorhabditis elegans ProteinsCryoelectron MicroscopyPhosphorylationProtein BindingAdaptor Protein Complex 2Adaptor Proteins, Vesicular TransportCaenorhabditis elegans ProteinsNCAP-1 protein, C elegansC. eleganscell biologyclathrin adaptorcryo-EMendocytosisgenetic screenmolecular biophysicsNECAPphosphorylationstructural biology

Identifiers

PMID31464684
PMCPMC6739873
OpenAlexW2971014682

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.