The International Journal of Developmental Biology

Int. J. Dev. Biol. 54: 1309 - 1315 (2010)

Vol 54, Issue 8-9

Drosophila Pelle phosphorylates Dichaete protein andinfluences its subcellular distribution in developing oocytes

Short Communication | Published: 30 April 2010

Mousumi Mutsuddi*,1, Ashim Mukherjee1, Baohe Shen3, James L. Manley3 and John R. Nambu*,2

1Department of Molecular and Human Genetics, Banaras Hindu University, Varanasi-221005, India, 2Department of Biology, University of Massachusetts, Amherst, MA, USA and 3Department of Biological Sciences, Columbia University, New York, NY, USA


The Drosophila Dichaete gene encodes a member of the Sox family of high mobility group (HMG) domain proteins that have crucial gene regulatory functions in diverse developmental processes. The subcellular localization and transcriptional regulatory activities of Sox proteins can be regulated by several post-translational modifications. To identify genes that functionally interact with Dichaete, we undertook a genetic modifier screen based on a Dichaete gain-of-function phenotype in the adult eye. Mutations in several genes, including decapentaplegic, engrailed and pelle, behaved as dominant modifiers of this eye phenotype. Further analysis of pelle mutants revealed that loss of pelle function results in alterations in the distinctive cytoplasmic distribution of Dichaete protein within the developing oocyte, as well as defects in the elaboration of individual egg chambers. The death domain-containing region of the Pelle protein kinase was found to associate with both Dichaete and mouse Sox2 proteins, and Pelle can phosphorylate Dichaete protein in vitro. Overall, these findings reveal that maternal functions of pelle are essential for proper localization of Dichaete protein in the oocyte and normal egg chamber formation. Dichaete appears to be a novel phosphorylation substrate for Pelle and may function in a Pelle-dependent signaling pathway during oogenesis.


Dichaete, Pelle, oogenesis, phosphorylation

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