The activity of the Drosophila Vestigial protein is modified by Scalloped-dependent phosphorylation

Virginia L. Pimmett, Hua Deng, Julie A. Haskins, Rebecca J. Mercier, Paul LaPointe, Andrew J. Simmonds

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

The Drosophila vestigial gene is required for proliferation and differentiation of the adult wing and for differentiation of larval and adult muscle identity. Vestigial is part of a multi-protein transcription factor complex, which includes Scalloped, a TEAD-class DNA binding protein. Binding Scalloped is necessary for translocation of Vestigial into the nucleus. We show that Vestigial is extensively post-translationally modified and at least one of these modifications is required for proper function during development. We have shown that there is p38-dependent phosphorylation of Serine 215 in the carboxyl-terminal region of Vestigial. Phosphorylation of Serine 215 occurs in the nucleus and requires the presence of Scalloped. Comparison of a phosphomimetic and non-phosphorylatable mutant forms of Vestigial shows differences in the ability to rescue the wing and muscle phenotypes associated with a null vestigial allele.

Original languageEnglish (US)
Pages (from-to)58-69
Number of pages12
JournalDevelopmental Biology
Volume425
Issue number1
DOIs
StatePublished - May 1 2017
Externally publishedYes

Keywords

  • Drosophila
  • P38
  • Scalloped
  • TEAD proteins
  • Vestigial
  • Vestigial-like

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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