Evidence map›Paper›PMID 21926430›Full record

ArticleThe Journal of biological chemistry2011

Sorting nexin 27 protein regulates trafficking of a p21-activated kinase (PAK) interacting exchange factor (β-Pix)-G protein-coupled receptor kinase interacting protein (GIT) complex via a PDZ domain interaction.

Julie L Valdes, Jingrong Tang, Mark I McDermott, Jean-Cheng Kuo, Seth P Zimmerman, Stephen M Wincovitch, Clare M Waterman, Sharon L Milgram, Martin P Playford

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

34 citing papers in PubMed, 45 citations in OpenAlex.

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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

9 authors at 2 institutions in 2 countries.

Julie L ValdesCell Biology and Physiology Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20982, USA.
Jingrong Tang
Mark I McDermott
Jean-Cheng Kuo
Seth P Zimmerman
Stephen M Wincovitch
Clare M Waterman
Sharon L Milgram
Martin P Playford
National Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

Mechanical Regulation of Cell AdhesionZIAHL005104 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI WATERMAN, CLARE MICHAL · 2009 to 2025
$30.9M
NHGRI/DIR Cytogenetics and Microscopy CoreZICHG200348 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI WINCOVITCH, STEPHEN · 2010 to 2025
$20.3M
Integration of Actin Dynamics and Adhesion in Cell MigrationZIAHL005105 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI WATERMAN, CLARE MICHAL · 2009 to 2025
$16.5M
The Cell Biology of Polarized CellsZIAHL005108 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MILGRAM, SHARON · 2009 to 2012
$3.0M
6 · The paper itself

Abstract

Sorting nexin 27 (SNX27) is a 62-kDa protein localized to early endosomes and known to regulate the intracellular trafficking of ion channels and receptors. In addition to a PX domain, SNX27 is the only sorting family member that contains a PDZ domain. To identify novel SNX27-PDZ binding partners, we performed a proteomic screen in mouse principal kidney cortical collecting duct cells using a GST-SNX27 fusion construct as bait. We found that β-Pix (p21-activated kinase-interactive exchange factor), a guanine nucleotide exchange factor for the Rho family of small GTPases known to regulate cell motility directly interacted with SNX27. The association of β-Pix and SNX27 is specific for β-Pix isoforms terminating in the type-1 PDZ binding motif (ETNL). In the same screen we also identified Git1/2 as a potential SNX27 interacting protein. The interaction between SNX27 and Git1/2 is indirect and mediated by β-Pix. Furthermore, we show recruitment of the β-Pix·Git complex to endosomal sites in a SNX27-dependent manner. Finally, migration assays revealed that depletion of SNX27 from HeLa and mouse principal kidney cortical collecting duct cells significantly decreases cell motility. We propose a model by which SNX27 regulates trafficking of β-Pix to focal adhesions and thereby influences cell motility.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsCell Cycle ProteinsCell MovementFocal AdhesionsGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsHeLa CellsHumansIntercellular Signaling Peptides and ProteinsKidney Tubules, CollectingMiceMultiprotein ComplexesNIH 3T3 CellsPDZ DomainsAdaptor Proteins, Signal TransducingARHGEF7 protein, humanCell Cycle ProteinsGIT1 protein, humanGit1 protein, mouseGIT2 protein, humanGit2 protein, mouseGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsIntercellular Signaling Peptides and ProteinsMultiprotein ComplexesPhosphoproteinsRho Guanine Nucleotide Exchange FactorsSNX27 protein, humanSnx27 protein, mouseSorting Nexins

Identifiers

PMID21926430
PMCPMC3234764
OpenAlexW1999151951

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.