Evidence map›Paper›PMID 26811329›Full record

ArticleMolecular and cellular biology2016

GGA3 Interacts with a G Protein-Coupled Receptor and Modulates Its Cell Surface Export.

Maoxiang Zhang, Jason E Davis, Chunman Li, Jie Gao, Wei Huang, Nevin A Lambert, Alvin V Terry, Guangyu Wu

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 25 citations in OpenAlex.

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  7. Human C1orf27 protein interacts with αThe Journal of biological chemistry · 2022
    Article
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  19. Regulation of αScientific reports · 2016
    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

8 authors at 1 institution in 1 country.

Maoxiang ZhangDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA.
Jason E DavisDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA.
Chunman LiDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA.
Jie GaoDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA.
Wei HuangDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA.
Nevin A LambertDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA.
Alvin V TerryDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA.
Guangyu WuDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, Georgia, USA guwu@gru.edu.
Augusta University · US

Funding

Cholinesterase Inhibitors, Axonal Transport, and MemoryR01ES012241 · NIEHS · UNIVERSITY OF GEORGIA (UGA) · PI TERRY, ALVIN V · 2004 to 2013
$2.8M
ER-to-Golgi traffic and signal regulation of GPCRsR01GM076167 · NIGMS · LSU HEALTH SCIENCES CENTER · PI WU, GUANGYU · 2006 to 2013
$2.2M
GPCR signaling complexes in living cellsR01GM078319 · NIGMS · AUGUSTA UNIVERSITY · PI LAMBERT, NEVIN ALAN · 2007 to 2017
$2.1M
NIEHS NIH HHS ES012241NIEHS NIH HHS R01 ES012241NIGMS NIH HHS GM076167NIGMS NIH HHS GM078319NIGMS NIH HHS R01 GM076167NIGMS NIH HHS R01 GM078319
6 · The paper itself

Abstract

Molecular mechanisms governing the anterograde trafficking of nascent G protein-coupled receptors (GPCRs) are poorly understood. Here, we have studied the regulation of cell surface transport of α2-adrenergic receptors (α2-ARs) by GGA3 (Golgi-localized, γ-adaptin ear domain homology, ADP ribosylation factor-binding protein 3), a multidomain clathrin adaptor protein that sorts cargo proteins at the trans-Golgi network (TGN) to the endosome/lysosome pathway. By using an inducible system, we demonstrated that GGA3 knockdown significantly inhibited the cell surface expression of newly synthesized α2B-AR without altering overall receptor synthesis and internalization. The receptors were arrested in the TGN. Furthermore, GGA3 knockdown attenuated α2B-AR-mediated signaling, including extracellular signal-regulated kinase 1/2 (ERK1/2) activation and cyclic AMP (cAMP) inhibition. More interestingly, GGA3 physically interacted with α2B-AR, and the interaction sites were identified as the triple Arg motif in the third intracellular loop of the receptor and the acidic motif EDWE in the VHS domain of GGA3. In contrast, α2A-AR did not interact with GGA3 and its cell surface export and signaling were not affected by GGA3 knockdown. These data reveal a novel function of GGA3 in export trafficking of a GPCR that is mediated via a specific interaction with the receptor.

Indexed as

Adaptor Proteins, Vesicular TransportAmino Acid SequenceBinding SitesCell LineCell MembraneGene Knockdown TechniquesHumansMolecular Sequence DataProtein Structure, TertiaryProtein TransportReceptors, Adrenergic, alpha-2Recombinant Fusion Proteinstrans-Golgi NetworkAdaptor Proteins, Vesicular TransportADRA2B protein, humanGGA adaptor proteinsReceptors, Adrenergic, alpha-2Recombinant Fusion Proteins

Identifiers

PMID26811329
PMCPMC4800796
OpenAlexW2268261757

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.