ArticleBiology open2012
The endocytic adapter E-Syt2 recruits the p21 GTPase activated kinase PAK1 to mediate actin dynamics and FGF signalling.
Article in Biology open, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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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.
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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.
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Who cites it
17 citing papers in PubMed, 19 citations in OpenAlex.
- A recombinant humanized type III collagen coating with anti-inflammatory and endothelialization-promoting effects for left atrial appendage closure devices.Regenerative biomaterials · 2026Article
- Characterization of clostridium botulinum neurotoxin serotype A (BoNT/A) and fibroblast growth factor receptor interactions using novel receptor dimerization assay.Scientific reports · 2021Article
- FGFR1 clustering with engineered tetravalent antibody improves the efficiency and modifies the mechanism of receptor internalization.Molecular oncology · 2020Article
- Targeting Cellular Trafficking of Fibroblast Growth Factor Receptors as a Strategy for Selective Cancer Treatment.Journal of clinical medicine · 2018Review
- Extended Synaptotagmin Localizes to Presynaptic ER and Promotes Neurotransmission and Synaptic Growth inGenetics · 2017Article
- The Extended-Synaptotagmins.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Antibody-induced dimerization of FGFR1 promotes receptor endocytosis independently of its kinase activity.Scientific reports · 2017Article
- A large-scale analysis of alternative splicing reveals a key role of QKI in lung cancer.Molecular oncology · 2016Article
- Loss of all 3 Extended Synaptotagmins does not affect normal mouse development, viability or fertility.Cell cycle (Georgetown, Tex.) · 2016Article
- Homeostatic regulation of the PI(4,5)P2-Ca(2+) signaling system at ER-PM junctions.Biochimica et biophysica acta · 2016Review
- Mechanisms of FGF gradient formation during embryogenesis.Seminars in cell & developmental biology · 2016Review
- The ER/PM microdomain, PI(4,5)P₂ and the regulation of STIM1-Orai1 channel function.Cell calcium · 2015Review
- Triggered Ca2+ influx is required for extended synaptotagmin 1-induced ER-plasma membrane tethering.The EMBO journal · 2015Article
- Extended Synaptotagmin Interaction with the Fibroblast Growth Factor Receptor Depends on Receptor Conformation, Not Catalytic Activity.The Journal of biological chemistry · 2015Article
- Unveiling physiological functions of extended synaptotagmins.Cell cycle (Georgetown, Tex.) · 2015Article
- Loss of Extended Synaptotagmins ESyt2 and ESyt3 does not affect mouse development or viability, but in vitro cell migration and survival under stress are affected.Cell cycle (Georgetown, Tex.) · 2014Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibroblast growth factor (FGF) signalling plays an essential role in early vertebrate development. However, the response to FGF requires endocytosis of the activated FGF receptor (FGFR) that is in part dependent on remodelling of the actin cytoskeleton. Recently we showed that the extended synaptotagmin family plasma membrane protein, E-Syt2, is an essential endocytic adapter for FGFR1. Here we show E-Syt2 is also an interaction partner for the p21-GTPase Activated Kinase PAK1. The phospholipid binding C2C domain of E-Syt2 specifically binds a site adjacent to the CRIB/GBD of PAK1. PAK1 and E-Syt2 selectively complex with FGFR1 and functionally cooperate in the FGF signalling. E-Syt2 binding suppresses actin polymerization and inhibits the activation of PAK1 by the GTPases Cdc42 and Rac. Interestingly, the E-Syt2 binding site on PAK1 extensively overlaps a site recently suggested to bind phospholipids. Our data suggest that PAK1 interacts with phospholipid membrane domains via E-Syt2, where it may cooperate in the E-Syt2-dependent endocytosis of activated FGFR1 by modulating cortical actin stability.
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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.