ArticlePloS one2012
Activation of endogenous FAK via expression of its amino terminal domain in Xenopus embryos.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 14 citations in OpenAlex.
- The apical ciliary adhesion complex is established at the basal foot of motile cilia and depends on the microtubule network.Scientific reports · 2022Article
- Wnt5b integrates Fak1a to mediate gastrulation cell movements via Rac1 and Cdc42.Open biology · 2020Article
- Addressing the Functional Determinants of FAK during Ciliogenesis in Multiciliated Cells.The Journal of biological chemistry · 2017Article
- Nuclear expression of Lyn, a Src family kinase member, is associated with poor prognosis in renal cancer patients.BMC cancer · 2016Article
- Kif2a depletion generates chromosome segregation and pole coalescence defects in animal caps and inhibits gastrulation of the Xenopus embryo.Molecular biology of the cell · 2015Article
- FAK is required for tension-dependent organization of collective cell movements in Xenopus mesendoderm.Developmental biology · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Focal Adhesion Kinase is a well studied tyrosine kinase involved in a wide number of cellular processes including cell adhesion and migration. It has also been shown to play important roles during embryonic development and targeted disruption of the FAK gene in mice results in embryonic lethality by day 8.5. PRINCIPAL
findingsHere we examined the pattern of phosphorylation of FAK during Xenopus development and found that FAK is phosphorylated on all major tyrosine residues examined from early blastula stages well before any morphogenetic movements take place. We go on to show that FRNK fails to act as a dominant negative in the context of the early embryo and that the FERM domain has a major role in determining FAK's localization at the plasma membrane. Finally, we show that autonomous expression of the FERM domain leads to the activation of endogenous FAK in a tyrosine 397 dependent fashion.
conclusionsOverall, our data suggest an important role for the FERM domain in the activation of FAK and indicate that integrin signalling plays a limited role in the in vivo activation of FAK at least during the early stages of development.
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