Evidence map›Paper›PMID 31040262›Full record

ArticleScience signaling2019

CD13 tethers the IQGAP1-ARF6-EFA6 complex to the plasma membrane to promote ARF6 activation, β1 integrin recycling, and cell migration.

Mallika Ghosh, Robin Lo, Ivan Ivic, Brian Aguilera, Veneta Qendro, Charan Devarakonda, Linda H Shapiro

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 43 citations in OpenAlex.

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  19. CD105Scientific reports · 2021
    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

7 authors at 1 institution in 1 country.

Mallika GhoshCenter for Vascular Biology, Department of Cell Biology, University of Connecticut School of Medicine, Farmington, CT 06032, USA. mghosh@uchc.edu lshapiro@uchc.edu.ORCID 0000-0002-5090-1275
Robin LoCenter for Vascular Biology, Department of Cell Biology, University of Connecticut School of Medicine, Farmington, CT 06032, USA.
Ivan IvicCenter for Vascular Biology, Department of Cell Biology, University of Connecticut School of Medicine, Farmington, CT 06032, USA.ORCID 0000-0003-4867-2829
Brian AguileraCenter for Vascular Biology, Department of Cell Biology, University of Connecticut School of Medicine, Farmington, CT 06032, USA.
Veneta QendroCenter for Vascular Biology, Department of Cell Biology, University of Connecticut School of Medicine, Farmington, CT 06032, USA.ORCID 0000-0001-7872-7785
Charan DevarakondaCenter for Vascular Biology, Department of Cell Biology, University of Connecticut School of Medicine, Farmington, CT 06032, USA.
Linda H ShapiroCenter for Vascular Biology, Department of Cell Biology, University of Connecticut School of Medicine, Farmington, CT 06032, USA. mghosh@uchc.edu lshapiro@uchc.edu.ORCID 0000-0003-4590-4671
University of Connecticut · US

Funding

Immune Evasion in Embryonic Stem Cell-based Tissue Repair and Transplantation.R01HL125186 · NHLBI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI FINCK, CHRISTINE M, SHAPIRO, LINDA H · 2015 to 2018
$1.9M
Endocytic Regulation of InflammationR01HL127449 · NHLBI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI SHAPIRO, LINDA H · 2015 to 2018
$1.7M
NHLBI NIH HHS R01 HL125186NHLBI NIH HHS R01 HL127449
6 · The paper itself

Abstract

Cell attachment to the extracellular matrix (ECM) requires a balance between integrin internalization and recycling to the surface that is mediated by numerous proteins, emphasizing the complexity of these processes. Upon ligand binding in various cells, the β1 integrin is internalized, traffics to early endosomes, and is returned to the plasma membrane through recycling endosomes. This trafficking process depends on the cyclical activation and inactivation of small guanosine triphosphatases (GTPases) by their specific guanine exchange factors (GEFs) and their GTPase-activating proteins (GAPs). In this study, we found that the cell surface antigen CD13, a multifunctional transmembrane molecule that regulates cell-cell adhesion and receptor-mediated endocytosis, also promoted cell migration and colocalized with β1 integrin at sites of cell adhesion and at the leading edge. A lack of CD13 resulted in aberrant trafficking of internalized β1 integrin to late endosomes and its ultimate degradation. Our data indicate that CD13 promoted ARF6 GTPase activity by positioning the ARF6-GEF EFA6 at the cell membrane. In migrating cells, a complex containing phosphorylated CD13, IQGAP1, GTP-bound (active) ARF6, and EFA6 at the leading edge promoted the ARF6 GTPase cycling and cell migration. Together, our findings uncover a role for CD13 in the fundamental cellular processes of receptor recycling, regulation of small GTPase activities, cell-ECM interactions, and cell migration.

Indexed as

Cell MovementADP-Ribosylation Factor 6ADP-Ribosylation FactorsAnimalsCD13 AntigensCell AdhesionCell Line, TumorCell MembraneEndocytosisEndosomesExtracellular MatrixGuanine Nucleotide Exchange FactorsHEK293 CellsHumansIntegrin beta1Mice, Inbred C57BLADP-Ribosylation Factor 6ADP-Ribosylation FactorsARF6 protein, humanArf6 protein, mouseCD13 AntigensGuanine Nucleotide Exchange FactorsIntegrin beta1IQ motif containing GTPase activating protein 1Monomeric GTP-Binding ProteinsMultiprotein Complexesras GTPase-Activating Proteins

Identifiers

PMID31040262
PMCPMC6756473
OpenAlexW2943301710

What OpenQuestion holds

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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.