Evidence map›Paper›PMID 31313456›Full record

ReviewTraffic (Copenhagen, Denmark)2019

Conformational regulation of AP1 and AP2 clathrin adaptor complexes.

Gwendolyn M Beacham, Edward A Partlow, Gunther Hollopeter

Open access · greenAbstract readReview
In one paragraph

Review in Traffic (Copenhagen, Denmark), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

38 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  15. Review
  16. 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
  17. Article
  18. Article
  19. Stepwise assembly of the AP2 endocytic clathrin adaptor complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

3 authors at 1 institution in 1 country.

Gwendolyn M BeachamDepartment of Molecular Medicine, Cornell University, Ithaca, New York.
Edward A PartlowDepartment of Molecular Medicine, Cornell University, Ithaca, New York.
Gunther HollopeterDepartment of Molecular Medicine, Cornell University, Ithaca, New York.ORCID 0000-0002-6409-0530
Cornell University · US

Funding

PREDOCTORAL TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM007273 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1985 to 2019
$11.6M
Molecular regulation of the AP2 clathrin adaptor complexR01GM127548 · NIGMS · CORNELL UNIVERSITY · PI HOLLOPETER, GUNTHER · 2019 to 2023
$2.1M
NIGMS NIH HHS R01 GM127548NIGMS NIH HHS T32 GM007273
6 · The paper itself

Abstract

Heterotetrameric clathrin adaptor protein complexes (APs) orchestrate the formation of coated vesicles for transport among organelles of the cell periphery. AP1 binds membranes enriched for phosphatidylinositol 4-phosphate, such as the trans Golgi network, while AP2 associates with phosphatidylinositol 4,5-bisphosphate of the plasma membrane. At their respective membranes, AP1 and AP2 bind the cytoplasmic tails of transmembrane protein cargo and clathrin triskelions, thereby coupling cargo recruitment to coat polymerization. Structural, biochemical and genetic studies have revealed that APs undergo conformational rearrangements and reversible phosphorylation to cycle between different activity states. While membrane, cargo and clathrin have been demonstrated to promote AP activation, growing evidence supports that membrane-associated proteins such as Arf1 and FCHo also stimulate this transition. APs may be returned to the inactive state via a regulated process involving phosphorylation and a protein called NECAP. Finally, because antiviral mechanisms often rely on appropriate trafficking of membrane proteins, viruses have evolved novel strategies to evade host defenses by influencing the conformation of APs. This review will cover recent advances in our understanding of the molecular inputs that stimulate AP1 and AP2 to adopt structurally and functionally distinct configurations.

Indexed as

Allosteric SiteAdaptor Protein Complex 1Adaptor Protein Complex 2Allosteric RegulationAnimalsClathrinHumansAdaptor Protein Complex 1Adaptor Protein Complex 2ClathrinAP1AP2Arf1clathrin adaptorsendocytosisFCHomuniscinsNECAPtetherin

Identifiers

PMID31313456
PMCPMC6774827
OpenAlexW2960136981

What OpenQuestion holds

Textmetadata
LicenceTDM
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.