ArticleTraffic (Copenhagen, Denmark)2014
Adaptor protein2 (AP2) orchestrates CXCR2-mediated cell migration.
Article in Traffic (Copenhagen, Denmark), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- The adaptor protein 2 (AP2) complex modulates habituation and behavioral selection across multiple pathways and time windows.iScience · 2024Article
- Endocytosis in cancer and cancer therapy.Nature reviews. Cancer · 2023Review
- Epigenetic Silencing ofCancers · 2023Article
- CXCL8 and the peritoneal metastasis of ovarian and gastric cancer.Frontiers in immunology · 2023Review
- CXCR2 Receptor: Regulation of Expression, Signal Transduction, and Involvement in Cancer.International journal of molecular sciences · 2022Review
- Dynamics and nanoscale organization of the postsynaptic endocytic zone at excitatory synapses.eLife · 2022Article
- The Cardiac Syndecan-2 Interactome.Frontiers in cell and developmental biology · 2020Article
- Endocytic Adaptor Proteins in Health and Disease: Lessons from Model Organisms and Human Mutations.Cells · 2019Review
- MicroRNA-regulated pathways of flow-stimulated angiogenesis and vascular remodeling in vivo.Journal of translational medicine · 2019Article
- Pancreatic islet inflammation: an emerging role for chemokines.Journal of molecular endocrinology · 2017Review
- Functional Genomics Identifies Tis21-Dependent Mechanisms and Putative Cancer Drug Targets Underlying Medulloblastoma Shh-Type Development.Frontiers in pharmacology · 2016Article
- Identification of key genes associated with colorectal cancer based on the transcriptional network.Pathology oncology research : POR · 2015Article
- On the move: endocytic trafficking in cell migration.Cellular and molecular life sciences : CMLS · 2015Review
- Control of CXCR2 activity through its ubiquitination on K327 residue.BMC cell biology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The chemokine receptor CXCR2 is vital for inflammation, wound healing, angiogenesis, cancer progression and metastasis. Adaptor protein 2 (AP2), a clathrin binding heterotetrameric protein comprised of α, β2, μ2 and σ2 subunits, facilitates clathrin-mediated endocytosis. Mutation of the LLKIL motif in the CXCR2 carboxyl-terminal domain (CTD) results in loss of AP2 binding to the receptor and loss of ligand-mediated receptor internalization and chemotaxis. AP2 knockdown also results in diminished ligand-mediated CXCR2 internalization, polarization and chemotaxis. Using knockdown/rescue approaches with AP2-μ2 mutants, the binding domains were characterized in reference to CXCR2 internalization and chemotaxis. When in an open conformation, μ2 Patch 1 and Patch 2 domains bind tightly to membrane PIP2 phospholipids. When AP2-μ2, is replaced with μ2 mutated in Patch 1 and/or Patch 2 domains, ligand-mediated receptor binding and internalization are not lost. However, chemotaxis requires AP2-μ2 Patch 1, but not Patch 2. AP2-σ2 has been demonstrated to bind dileucine motifs to facilitate internalization. Expression of AP2-σ2 V88D and V98S dominant negative mutants resulted in loss of CXCR2 mediated chemotaxis. Thus, AP2 binding to both membrane phosphatidylinositol phospholipids and dileucine motifs is crucial for directional migration or chemotaxis. Moreover, AP2-mediated receptor internalization can be dissociated from AP2-mediated chemotaxis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.