The JIL-1 kinase interacts with lamin Dm0 and regulates nuclear lamina morphology of Drosophila nurse cells

Xiaomin Bao, Weiguo Zhang, Robert Krencik, Huai Deng, Yanming Wang, Jack Girton, Jørgen Johansen, Kristen M Johansen

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


We have used a yeast two-hybrid screen to identify lamin Dm0 as an interaction partner for the nuclear JIL-1 kinase. This molecular interaction was confirmed by GST-fusion protein pull-down assays and by co-immunoprecipitation experiments. Using deletion construct analysis we show that a predicted globular domain of the basic region of the COOH-terminal domain of JIL-1 was sufficient for mediating the molecular interactions with lamin Dm0. A reciprocal analysis with truncated lamin Dm0 constructs showed that the interaction with JIL-1 required sequences in the tail domain of lamin Dm0 that include the Ig-like fold. Further support for a molecular interaction between JIL-1 and lamin Dm0 in vivo was provided by genetic interaction assays. We show that nuclear positioning and lamina morphology were abnormal in JIL-1 mutant egg chambers. The most common phenotypes observed were abnormal nurse cell nuclear lamina protrusions through the ring canals near the oocyte, as well as dispersed and mislocalized lamin throughout the egg chamber. These phenotypes were completely rescued by a full-length JIL-1 transgenic construct. Thus, our results suggest that the JIL-1 kinase is required to maintain nuclear morphology and integrity of nurse cells during oogenesis and that this function may be linked to molecular interactions with lamin Dm0.

Original languageEnglish (US)
Pages (from-to)5079-87
Number of pages9
JournalJournal of Cell Science
Issue numberPt 21
StatePublished - Nov 1 2005


  • Alleles
  • Animals
  • Animals, Genetically Modified
  • Cell Nucleus
  • Drosophila Proteins
  • Drosophila melanogaster
  • Lamins
  • Mutation
  • Peptide Fragments
  • Protein Interaction Mapping
  • Protein Structure, Tertiary
  • Ribosomal Protein S6 Kinases, 90-kDa
  • Two-Hybrid System Techniques
  • Journal Article
  • Research Support, N.I.H., Extramural


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