Evidence map›Paper›PMID 12604586›Full record

ArticleThe Journal of cell biology2003

AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation.

Pradipta Ghosh, Stuart Kornfeld

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
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  5. Synthesis of a 3,7-Disubstituted Isothiazolo[4,3-Molecules (Basel, Switzerland) · 2024
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  8. Review
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  17. Bidirectional apical-basal traffic of the cation-independent mannose-6-phosphate receptor in brain endothelial cells.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2017
    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

2 authors at 1 institution in 1 country.

Pradipta GhoshWashington University School of Medicine, Department of Internal Medicine, 660 S. Euclid Ave., Box 8125, St. Louis, MO 63110, USA.
Stuart Kornfeld
Washington University in St. Louis · US

Funding

STRUCTURE, BIOSYNTHESIS &FUNCTION OF GLYCOPROTEINSR37CA008759 · NCI · WASHINGTON UNIVERSITY · PI KORNFELD, STUART A · 1990 to 2018
$14.0M
Structure, Biosynthesis & Function of GlycoproteinsR01CA008759 · NCI · WASHINGTON UNIVERSITY · PI KORNFELD, STUART A · 1985 to 2023
$3.5M
NCI NIH HHS R01 CA008759NCI NIH HHS R01 CA-08759NCI NIH HHS R37 CA008759
6 · The paper itself

Abstract

The adaptor protein complex-1 (AP-1) sorts and packages membrane proteins into clathrin-coated vesicles (CCVs) at the TGN and endosomes. Here we show that this process is highly regulated by phosphorylation of AP-1 subunits. Cell fractionation studies revealed that membrane-associated AP-1 differs from cytosolic AP-1 in the phosphorylation status of its beta1 and mu1 subunits. AP-1 recruitment onto the membrane is associated with protein phosphatase 2A (PP2A)-mediated dephosphorylation of its beta1 subunit, which enables clathrin assembly. This Golgi-associated isoform of PP2A exhibits specificity for phosphorylated beta1 compared with phosphorylated mu1. Once on the membrane, the mu1 subunit undergoes phosphorylation, which results in a conformation change, as revealed by increased sensitivity to trypsin. This conformational change is associated with increased binding to sorting signals on the cytoplasmic tails of cargo molecules. Dephosphorylation of mu1 (and mu2) by another PP2A-like phosphatase reversed the effect and resulted in adaptor release from CCVs. Immunodepletion and okadaic acid inhibition studies demonstrate that PP2A is the cytosolic cofactor for Hsc-70-mediated adaptor uncoating. A model is proposed where cyclical phosphorylation/dephosphorylation of the subunits of AP-1 regulate its function from membrane recruitment until its release into cytosol.

Indexed as

Adaptor Protein Complex 1AnimalsBinding SitesCatalytic DomainCattleCell MembraneClathrin-Coated VesiclesCytosolEnzyme InhibitorsEukaryotic CellsGolgi ApparatusHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsL CellsLigandsMiceAdaptor Protein Complex 1Enzyme InhibitorsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHspa8 protein, mouseLigandsOkadaic AcidPhosphoprotein PhosphatasesProtein Phosphatase 2

Identifiers

PMID12604586
PMCPMC2173368
OpenAlexW2158907019

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.