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Embryonic axis formation relies on the Huluwa (Hwa) protein. Phosphorylation of Hwa at Ser168 is crucial for activating beta-catenin signaling and inducing body axes in vertebrates.

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Area of Science:

  • Developmental biology
  • Molecular biology
  • Cell signaling

Background:

  • Embryonic axis formation is critical for vertebrate development and patterning.
  • The dorsal organizer and maternally derived Huluwa (Hwa) protein are key regulators.
  • The precise mechanism of Hwa activation and regulation was previously unknown.

Purpose of the Study:

  • To elucidate the regulatory mechanism of Huluwa (Hwa) protein activity.
  • To identify key residues and signaling pathways involved in Hwa-mediated axis induction.
  • To understand the role of Hwa phosphorylation in embryonic development.

Main Methods:

  • Candidate screening to identify critical Hwa mutations.
  • Biochemical assays to assess protein binding and degradation (Tankyrase 1/2, Axin).
  • In vitro and in vivo kinase assays and phosphorylation studies.
  • Generation of knock-in alleles and antibody treatments.

Main Results:

  • A mutation at Ser168 in the PPNSP motif abolished Hwa's axis-inducing activity.
  • Ser168 phosphorylation was found to enhance Hwa activity and beta-catenin signaling.
  • Multiple kinases (Cdk16, Cdk2, GSK3β) were identified as regulators of Ser168 phosphorylation.
  • Mutating Ser168 to alanine in knock-in embryos resulted in a complete loss of body axes.

Conclusions:

  • Serine 168 (Ser168) phosphorylation acts as a critical switch for Huluwa (Hwa) protein function.
  • Hwa/beta-catenin signaling is tightly regulated by kinase-mediated phosphorylation at Ser168 for embryonic axis induction.
  • This phosphorylation mechanism is essential for vertebrate embryonic development and patterning.