The Drosophila Fry protein interacts with Trc and is highly mobile in vivo
1 Biology Department, Cell Biology Department, Cancer Center, Morphogenesis and Regenerative Medicine Institute, University of Virginia, Charlottesville, VA 22903, USA
2 Neural Morphogenesis Laboratory, National Institute of Genetics, Yata 1111, Mishima, Shizuoka 411-8540, Japan
3 Howard Hughes Medical Institute, Departments of Physiology, Biochemistry, and Biophysics, University of California San Francisco, San Francisco, CA 94143, USA
BMC Developmental Biology 2010, 10:40 doi:10.1186/1471-213X-10-40Published: 20 April 2010
Cell polarity is a common feature of eukaryotic cells. The NDR kinases have been found to regulate polarized growth in both animal cells and fungi. Drosophila Tricornered is an NDR kinase that is essential for the normal polarized growth of extensions of epidermal cells and for the tiling and branching of dendrites of da sensory neurons. Tricornered function requires interacting with the large Furry protein (3479 amino acid).
We constructed a furry (fry) transgene and established that it rescued the lethality of fry null mutations. The encoded protein was tagged at both its amino and carboxy termini and this allowed us to demonstrate that the protein existed as an uncleaved protein in vivo. We used the C terminal GFP tag to follow the protein in vivo and found it to be highly mobile. Interestingly Fry accumulated at the distal tip of growing bristles. We established that Fry and Trc could be co-immunoprecipitated from wing discs.
The mobility of Fry in both bristles and dendrites suggests that it could function in directing/mediating the intracellular transport needed for polarized growth. Our observations that full length Fry and Trc show only partial co-localization in growing bristles while an amino terminal fragment of Fry shows close to complete co-localization with Trc suggests that the interaction between these proteins is transient and regulated.