These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Phosphorylation of phospholipase C gamma 1 and its association with the FGF receptor is developmentally regulated and occurs during mesoderm induction in Xenopus laevis.
    Author: Ryan PJ, Gillespie LL.
    Journal: Dev Biol; 1994 Nov; 166(1):101-11. PubMed ID: 7958437.
    Abstract:
    We have examined phosphorylation of phospholipase C gamma 1 (PLC gamma 1) and its association with FGFR1 during mesoderm induction in animal pole explants and during early development in Xenopus embryos. In explants, PLC gamma 1 became associated with FGFR1 during mesoderm induction by FGF or by vegetal cells, the source of the natural inducer. Both PLC gamma 1 and FGFR1 were phosphorylated on tyrosine, indicating that both proteins were activated. Phosphorylation of these two proteins occurred very early during the induction process (within 0.5 hr), providing evidence that a member of the FGF family is a component of the vegetal inducing signal. PLC gamma 1 was also associated with FGFR1 in Xenopus blastulae and this association was specific to presumptive mesoderm cells. Examination of the PLC gamma 1 phosphorylation pattern during early Xenopus development and its association with FGFR1 revealed that maximum phosphorylation and association of these two proteins occurred during early- to mid-blastula stages, concurrent with mesoderm induction in vivo. This spatiotemporal pattern PLC gamma 1-FGFR1 association and phosphorylation suggests that PLC gamma 1 is involved in intracellular signaling during mesoderm induction in Xenopus. Seven additional phosphotyrosyl bands were coimmunoprecipitated with either PLC gamma 1 or FGFR1 from Xenopus blastulae; these bands may represent additional components of an FGFR1 signaling complex. One of these phosphotyrosyl bands was identified as NCK. In addition, growth factor receptor-binding protein, and son-of-sevenless two upstream regulators of RAS signaling, were co-immunoprecipitated with FGFR1.
    [Abstract] [Full Text] [Related] [New Search]