The Drosophila Fry protein interacts with Trc and is highly mobile in vivo
書誌事項
- 公開日
- 2010-04-20
- DOI
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- 10.1186/1471-213x-10-40
- 公開者
- Springer Science and Business Media LLC
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説明
<jats:title>Abstract</jats:title> <jats:sec> <jats:title>Background</jats:title> <jats:p>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).</jats:p> </jats:sec> <jats:sec> <jats:title>Results</jats:title> <jats:p>We constructed a <jats:italic>furry</jats:italic> (<jats:italic>fry</jats:italic>) transgene and established that it rescued the lethality of <jats:italic>fry</jats:italic> 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.</jats:p> </jats:sec> <jats:sec> <jats:title>Conclusions</jats:title> <jats:p>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.</jats:p> </jats:sec>
収録刊行物
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- BMC Developmental Biology
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BMC Developmental Biology 10 (1), 40-, 2010-04-20
Springer Science and Business Media LLC