Journal
DEVELOPMENT
Volume 148, Issue 10, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/dev.199441
Keywords
FGF receptor; FGF signal; Xenopus; Kindlin2; Neural crest
Categories
Funding
- National Key R&D Program of China [2016YFE0204700]
- National Key R&D Program of China, Synthetic Biology Research [2019YFA0904500]
- Research Grants Council of Hong Kong [14167017, 14112618]
- International Partnership Program of Chinese Academy of Sciences [152453KYSB20170031]
- Guangdong Natural Science Foundation [2017A030313209]
- Guangdong Provincial Key Laboratory of Cell Microenvironment and Disease Research [2017B030301018]
- Key Research and Development Program of Ningxia Province [2019BEH03003]
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Kindlin2 is essential for neural crest formation in Xenopus embryos independently of integrins, and it regulates the FGF pathway to promote the stability of FGF receptor 1.
The focal adhesion protein Kindlin2 is essential for integrin activation, a process that is fundamental to cell-extracellular matrix adhesion. Kindlin 2 (Fermt2) is widely expressed in mouse embryos, and its absence causes lethality at the peri-implantation stage due to the failure to trigger integrin activation. The function of kindlin2 during embryogenesis has not yet been fully elucidated as a result of this early embryonic lethality. Here, we showedthat kindlin2isessential forneural crest (NC) formationinXenopus embryos. Loss-of-function assays performed with kindlin2-specific morpholino antisense oligos (MOs) or with CRISPR/Cas9 techniques in Xenopus embryos severely inhibit the specification of the NC. Moreover, integrin-binding-deficient mutants of Kindlin2 rescued the phenotype caused by loss of kindlin2, suggesting that the function of kindlin2 during NCspecification is independent of integrins. Mechanistically, we found that Kindlin2 regulates the fibroblast growth factor (FGF) pathway, and promotes the stability of FGF receptor 1. Our study reveals a novel function of Kindlin2 in regulating the FGF signaling pathway and provides mechanistic insights into the function of Kindlin2 during NC specification.
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