ArticleNature structural & molecular biology2016
Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 40 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
40 citing papers in PubMed, 80 citations in OpenAlex.
- AAK1-mediated phosphorylation of PDLIM5 and Talin1 promotes focal adhesion disassembly to accelerate cell migration.Nature communications · 2026Article
- Regulation of cell dynamics by rapid integrin transport through the biosynthetic pathway.The Journal of cell biology · 2026Article
- The EV-mitochondrial outsourcing network as a therapeutic target for age-related testosterone deficiency: from network collapse to clinical intervention.Frontiers in endocrinology · 2026Review
- Crystal structures of the μ2 subunit of clathrin-adaptor protein 2 in complex with peptides derived from human papillomavirus 16 E7.Journal of microbiology (Seoul, Korea) · 2025Article
- UBE2V1 governs aging induced protein aggregation and developmental defects in oocytes and embryos.Communications biology · 2025Article
- The essential clathrin adapter protein complex-2 is tumor suppressive specifically in vivo.Nature communications · 2025Article
- The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025Review
- IGFBP5 is released by senescent cells and is internalized by healthy cells, promoting their senescence through interaction with retinoic receptors.Cell communication and signaling : CCS · 2024Article
- Single-cell transcriptome sequencing reveals aberrantly activated inter-tumor cell signaling pathways in the development of clear cell renal cell carcinoma.Journal of translational medicine · 2024Article
- Ectocytosis renders T cell receptor signaling self-limiting at the immune synapse.Science (New York, N.Y.) · 2023Article
- Organization, dynamics and mechanoregulation of integrin-mediated cell-ECM adhesions.Nature reviews. Molecular cell biology · 2023Review
- Force tuning through regulation of clathrin-dependent integrin endocytosis.The Journal of cell biology · 2023Article
- Linc00662 mAmerican journal of cancer research · 2023Article
- Use of Ecto-Tagged Integrins to Monitor Integrin Exocytosis and Endocytosis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- FCHO controls AP2's initiating role in endocytosis through a PtdIns(4,5)PScience advances · 2022Article
- Cooperation of cell adhesion and autophagy in the brain: Functional roles in development and neurodegenerative disease.Matrix biology plus · 2021Review
- Article
- Myosin-X and talin modulate integrin activity at filopodia tips.Cell reports · 2021Article
- SH3BP4 promotes neuropilin-1 and α5-integrin endocytosis and is inhibited by Akt.Developmental cell · 2021Article
- Cytoplasmic short linear motifs in ACE2 and integrin βScience signaling · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
Integrins are heterodimeric cell-surface adhesion molecules comprising one of 18 possible α-chains and one of eight possible β-chains. They control a range of cell functions in a matrix- and ligand-specific manner. Integrins can be internalized by clathrin-mediated endocytosis (CME) through β subunit-based motifs found in all integrin heterodimers. However, whether specific integrin heterodimers can be selectively endocytosed was unknown. Here, we found that a subset of α subunits contain an evolutionarily conserved and functional YxxΦ motif directing integrins to selective internalization by the most abundant endocytic clathrin adaptor, AP2. We determined the structure of the human integrin α4-tail motif in complex with the AP2 C-μ2 subunit and confirmed the interaction by isothermal titration calorimetry. Mutagenesis of the motif impaired selective heterodimer endocytosis and attenuated integrin-mediated cell migration. We propose that integrins evolved to enable selective integrin-receptor turnover in response to changing matrix conditions.
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.