EAST interacts with Megator and localizes to the putative spindle matrix during mitosis in Drosophila.
We have used immunocytochemistry to demonstrate that the EAST protein in Drosophila, which forms an expandable nuclear endoskeleton at interphase, redistributes during mitosis to colocalize with the spindle matrix proteins, Megator and Skeletor. EAST and Megator also colocalize to the intranuclear space surrounding the chromosomes at interphase. EAST is a novel protein that does not have any previously characterized motifs or functional domains. However, we show by immunoprecipitation experiments that EAST is likely to molecularly interact with Megator which has a large NH2-terminal coiled-coil domain with the capacity for self assembly. On the basis of these findings, we propose that Megator and EAST interact to form a nuclear endoskeleton and as well are important components of the putative spindle matrix complex during mitosis.
Qi
Hongying
H
Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
Rath
Uttama
U
Ding
Yun
Y
Ji
Yun
Y
Blacketer
Melissa J
MJ
Girton
Jack
J
Johansen
Jørgen
J
Johansen
Kristen M
KM
D000818:Animals; D018797:Cell Cycle Proteins; D029721:Drosophila Proteins / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000166:cytology* / Q000378:metabolism*; D008938:Mitosis; D034521:Nuclear Matrix-Associated Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D011485:Protein Binding; D008941:Spindle Apparatus / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism
D018797:Cell Cycle Proteins; D029721:Drosophila Proteins; C114107:EAST protein, Drosophila; C498867:Mtor protein, Drosophila; D034521:Nuclear Matrix-Associated Proteins; D010750:Phosphoproteins; D014404:Tubulin