Evidence map›Paper›PMID 22343291›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Basolateral sorting of the coxsackie and adenovirus receptor through interaction of a canonical YXXPhi motif with the clathrin adaptors AP-1A and AP-1B.

Jose Maria Carvajal-Gonzalez, Diego Gravotta, Rafael Mattera, Fernando Diaz, Andres Perez Bay, Angel C Roman, Ryan P Schreiner, Roland Thuenauer, Juan S Bonifacino, Enrique Rodriguez-Boulan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

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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

10 authors.

Jose Maria Carvajal-GonzalezDepartment of Ophthalmology, Margaret Dyson Vision Research Institute, Weill Cornell Medical College, New York, NY 10065, USA.
Diego Gravotta
Rafael Mattera
Fernando Diaz
Andres Perez Bay
Angel C Roman
Ryan P Schreiner
Roland Thuenauer
Juan S Bonifacino
Enrique Rodriguez-Boulan

Funding

Protein Trafficking In The Endosomal-Lysosomal SystemZIAHD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2025
$48.3M
RETINA--REVERSED POLARITY IN RPER01EY008538 · NEI · WEILL MEDICAL COLL OF CORNELL UNIV · PI RODRIGUEZ-BOULAN, ENRIQUE J · 1991 to 2020
$13.4M
SORTING OF PLASMA MEMBRANE PROTEINS IN EPITHELIAL CELLSR01GM034107 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI RODRIGUEZ-BOULAN, ENRIQUE J · 1985 to 2019
$9.6M
Intramural NIH HHSNEI NIH HHS EY08538NEI NIH HHS R01 EY008538NIGMS NIH HHS GM34107NIGMS NIH HHS R01 GM034107
6 · The paper itself

Abstract

The coxsackie and adenovirus receptor (CAR) plays key roles in epithelial barrier function at the tight junction, a localization guided in part by a tyrosine-based basolateral sorting signal, (318)YNQV(321). Sorting motifs of this type are known to route surface receptors into clathrin-mediated endocytosis through interaction with the medium subunit (μ2) of the clathrin adaptor AP-2, but how they guide new and recycling membrane proteins basolaterally is unknown. Here, we show that YNQV functions as a canonical YxxΦ motif, with both Y318 and V321 required for the correct basolateral localization and biosynthetic sorting of CAR, and for interaction with a highly conserved pocket in the medium subunits (μ1A and μ1B) of the clathrin adaptors AP-1A and AP-1B. Knock-down experiments demonstrate that AP-1A plays a role in the biosynthetic sorting of CAR, complementary to the role of AP-1B in basolateral recycling of this receptor. Our study illustrates how two clathrin adaptors direct basolateral trafficking of a plasma membrane protein through interaction with a canonical YxxΦ motif.

Indexed as

Adaptor Protein Complex 1Adaptor Protein Complex 2Amino Acid MotifsAnimalsCell LineCell MembraneClathrinCoxsackie and Adenovirus Receptor-Like Membrane ProteinDogsEndocytosisEndosomesEpithelial CellsExocytosisFishesGreen Fluorescent ProteinsHumansAdaptor Protein Complex 1Adaptor Protein Complex 2ClathrinCLMP protein, humanCoxsackie and Adenovirus Receptor-Like Membrane ProteinGreen Fluorescent ProteinsReceptors, Virus

Identifiers

PMID22343291
PMCPMC3309744

What OpenQuestion holds

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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.