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PLoS One ; 9(9): e106112, 2014.
Article in English | MEDLINE | ID: mdl-25203404

ABSTRACT

Little is known about how microtubules are regulated in different cell types during development. EB1 plays a central role in the regulation of microtubule plus ends. It directly binds to microtubule plus ends and recruits proteins which regulate microtubule dynamics and behaviour. We report the identification of Kank, the sole Drosophila orthologue of human Kank proteins, as an EB1 interactor that predominantly localises to embryonic attachment sites between muscle and tendon cells. Human Kank1 was identified as a tumour suppressor and has documented roles in actin regulation and cell polarity in cultured mammalian cells. We found that Drosophila Kank binds EB1 directly and this interaction is essential for Kank localisation to microtubule plus ends in cultured cells. Kank protein is expressed throughout fly development and increases during embryogenesis. In late embryos, it accumulates to sites of attachment between muscle and epidermal cells. A kank deletion mutant was generated. We found that the mutant is viable and fertile without noticeable defects. Further analysis showed that Kank is dispensable for muscle function in larvae. This is in sharp contrast to C. elegans in which the Kank orthologue VAB-19 is required for development by stabilising attachment structures between muscle and epidermal cells.


Subject(s)
Drosophila Proteins/metabolism , Drosophila melanogaster/embryology , Drosophila melanogaster/metabolism , Microtubule-Associated Proteins/metabolism , Muscles/embryology , Tendons/embryology , Tumor Suppressor Proteins/metabolism , Active Transport, Cell Nucleus , Adaptor Proteins, Signal Transducing , Amino Acid Sequence , Animals , Cell Nucleus/metabolism , Cytoskeletal Proteins , Drosophila Proteins/chemistry , Drosophila melanogaster/physiology , Female , Fertility , Gene Expression Regulation, Developmental , Humans , Male , Microtubules/metabolism , Muscles/metabolism , Tendons/metabolism , Tumor Suppressor Proteins/chemistry
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