ArticleMolecular biology of the cell2007
EphA4 signaling regulates blastomere adhesion in the Xenopus embryo by recruiting Pak1 to suppress Cdc42 function.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Modulating PAK1: Accessory Proteins as Promising Therapeutic Targets.Biomolecules · 2025Review
- Article
- Article
- Nck adaptors at a glance.Journal of cell science · 2021Article
- A cancer mutation promotes EphA4 oligomerization and signaling by altering the conformation of the SAM domain.The Journal of biological chemistry · 2021Article
- Protein context shapes the specificity of SH3 domain-mediated interactions in vivo.Nature communications · 2021Article
- The Evolutionary History of Ephs and Ephrins: Toward Multicellular Organisms.Molecular biology and evolution · 2020Article
- Proteomic Analysis of NCK1/2 Adaptors Uncovers Paralog-specific Interactions That Reveal a New Role for NCK2 in Cell Abscission During Cytokinesis.Molecular & cellular proteomics : MCP · 2018Article
- Direct Phosphorylation of SRC Homology 3 Domains by Tyrosine Kinase Receptors Disassembles Ligand-Induced Signaling Networks.Molecular cell · 2018Article
- Variable combinations of specific ephrin ligand/Eph receptor pairs control embryonic tissue separation.PLoS biology · 2014Article
- A conserved Oct4/POUV-dependent network links adhesion and migration to progenitor maintenance.Current biology : CB · 2013Article
- PAK-PIX interactions regulate adhesion dynamics and membrane protrusion to control neurite outgrowth.Journal of cell science · 2013Article
- Global evaluation of Eph receptors and ephrins in lung adenocarcinomas identifies EphA4 as an inhibitor of cell migration and invasion.Molecular cancer therapeutics · 2012Article
- The endocytic adapter E-Syt2 recruits the p21 GTPase activated kinase PAK1 to mediate actin dynamics and FGF signalling.Biology open · 2012Article
- Eph-dependent cell-cell adhesion and segregation in development and cancer.Cellular and molecular life sciences : CMLS · 2012Review
- Eph/ephrin signaling in cell-cell and cell-substrate adhesion.Frontiers in bioscience (Landmark edition) · 2012Review
- The Caenorhabditis elegans Eph receptor activates NCK and N-WASP, and inhibits Ena/VASP to regulate growth cone dynamics during axon guidance.PLoS genetics · 2012Article
- An RNA interference phenotypic screen identifies a role for FGF signals in colon cancer progression.PloS one · 2011Article
- Myosin-X is critical for migratory ability of Xenopus cranial neural crest cells.Developmental biology · 2009Article
- PAK thread from amoeba to mammals.Journal of cellular biochemistry · 2009Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The control of cell adhesion is an important mechanism by which Eph receptors regulate cell sorting during development. Activation of EphA4 in Xenopus blastulae induces a reversible, cell autonomous loss-of-adhesion and disruption of the blastocoel roof. We show this phenotype is rescued by Nckbeta (Grb4) dependent on its interaction with EphA4. Xenopus p21(Cdc42/Rac)-activated kinase xPAK1 interacts with Nck, is activated in embryo by EphA4 in an Nck-dependent manner, and is required for EphA4-induced loss-of-adhesion. Ectopic expression of xPAK1 phenocopies EphA4 activation. This does not require the catalytic activity of xPAK1, but it does require its GTPase binding domain and is enhanced by membrane targeting. Indeed, membrane targeting of the GTPase binding domain (GBD) of xPAK1 alone is sufficient to phenocopy EphA4 loss-of-adhesion. Both EphA4 and the xPAK1-GBD down-regulate RhoA-GTP levels, and consistent with this, loss-of-adhesion can be rescued by activated Cdc42, Rac, and RhoA and can be epistatically induced by dominant-negative RhoA. Despite this, neither Cdc42 nor Rac activities are down-regulated by EphA4 activation or by the xPAK1-GBD. Together, the data suggest that EphA4 activation sequesters active Cdc42 and in this way down-regulates cell-cell adhesion. This novel signaling pathway suggests a mechanism for EphA4-guided migration.
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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.