BAG6 is a novel microtubule-binding protein that regulates ciliogenesis by modulating the cell cycle and interacting with ?-tubulin.

Microtubule-binding proteins provide an alternative and vital pathway to the functional diversity of microtubules. Considerable work is still required to understand the complexities of microtubule-associated cellular processes and to identify novel microtubule-binding proteins. In this study, we identify Bcl2-associated athanogene cochaperone 6 (BAG6) as a novel microtubule-binding protein and reveal ...
that it is crucial for primary ciliogenesis. By immunofluorescence we show that BAG6 largely colocalizes with intracellular microtubules and by co-immunoprecipitation we demonstated that it can interact with ?-tubulin. Additionally, both the UBL and BAG domains of BAG6 are indispensable for its interaction with ?-tubulin. Moreover, the assembly of primary cilia in RPE-1 cells is significantly inhibited upon the depletion of BAG6. Notably, BAG6 inhibition leads to an abnormal G0/G1 transition during the cell cycle. In addition, BAG6 colocalizes and interactes with the centrosomal protein ?-tubulin, suggesting that BAG6 might regulate primary ciliogenesis through its action in centrosomal function. Collectively, our findings suggest that BAG6 is a novel microtubule-bindng protein crucial for primary ciliogenesis.
Mesh Terms:
Carrier Proteins, Cell Line, Cell Line, Tumor, G1 Phase, HEK293 Cells, HeLa Cells, Humans, Microtubule-Associated Proteins, Microtubules, Molecular Chaperones, Protein Binding, Resting Phase, Cell Cycle, Tubulin
Exp Cell Res
Date: Dec. 01, 2019
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