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Histochemistry and Cell Biology

, Volume 145, Issue 1, pp 5–16

First Online: 26 October 2015Accepted: 20 September 2015DOI: 10.1007-s00418-015-1368-5

Cite this article as: Chen, J., Balakrishnan-Renuka, A., Hagemann, N. et al. Histochem Cell Biol 2016 145: 5. doi:10.1007-s00418-015-1368-5

Abstract

ATOH8 is a bHLH transcription factor playing roles in a variety of developmental processes such as neurogenesis, differentiation of pancreatic precursor cells, development of kidney and muscle, and differentiation of endothelial cells. PPP3CB belongs to the catalytic subunit of the serine-threonine phosphatase, calcineurin, which can dephosphorylate its substrate proteins to regulate their physiological activities. In our study, we demonstrated that ATOH8 interacts with PPP3CB in vitro with different approaches. We show that the conserved catalytic domain of PPP3CB interacts with both the N-terminus and the bHLH domain of ATOH8. Although the interaction domain of PPP3CB is conserved among all isoforms of calcineurin A, ATOH8 selectively interacts with PPP3CB instead of PPP3CA, probably due to the unique proline-rich region present in the N-terminus of PPP3CB, which controls the specificity of its interaction partners. Furthermore, we show that inhibition of the interaction with calcineurin inhibitor, cyclosporin A CsA, leads to the retention of ATOH8 to the cytoplasm, suggesting that the interaction renders nuclear localization of ATOH8 which may be critical to control its activity as transcription factor.

KeywordsATOH8 PPP3CB Calcineurin Cyclosporin A Electronic supplementary materialThe online version of this article doi:10.1007-s00418-015-1368-5 contains supplementary material, which is available to authorized users.

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Author: Jingchen Chen - Ajeesh Balakrishnan-Renuka - Nina Hagemann - Carsten Theiss - Verena Chankiewitz - Jinzhong Chen - Qin Pu -

Source: https://link.springer.com/







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