706C Poster - 11. Cell division and cell growth
Saturday April 09, 1:30 PM - 3:30 PM

Functional domains of the Ana1 centriole protein and their regulation by mitotic protein kinases and phosphatases


Authors:
Agota Nagy 1; Nikola Dzhindzhev 2; Pallavi Panda 1; Levente Kovacs 1; Helene Rangone 2; Jingyan Fu 2,3; Zoltan Lipinszki 2,4; David Glover 1,2

Affiliations:
1) Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California, USA; 2) Department of Genetics, University of Cambridge, Cambridge, UK; 3) State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China; 4) Biological Research Centre, Institute of Biochemistry, MTA Lendület Laboratory of Cell Cycle Regulation, Szeged, Hungary

Keywords:
d. centrosome; i. cellular organelles

Centrioles are evolutionary conserved, 9-fold symmetrical structures that form the core component of centrosomes and also serve as basal bodies for cilia and flagella. They play critical roles in cell division, motility and signalling. The assembly of centrioles through the cell cycle is tightly regulated, leading to their elongation in the G2 phase followed by their conversion to centrosomes during mitosis. These processes require the progressive assembly of a network of interacting proteins, which extend from the inside to the outside of the centriole. Here we focus on Ana1, the protein that links the inner and outer centriole components of this molecular network. We wish to understand the independent function of Ana1’s domains and to this end, have created transgenic flies expressing N-and C-terminal fragments of different lengths. We separately express these fragments in different ana1 mutant backgrounds and determine the extent to which they can function independently to drive centriole duplication and elongation in different tissues. We are determining how the interactions of Ana1’s different functional domains with other key centriole proteins are dependent upon phosphorylation by mitotic protein kinases for completion of the procentriole, its disengagement from the mother centriole, and recruitment of peri-centriolar material and how protein phosphatases ensure the cyclical nature of some of these interactions.