A novel interaction between ATOH8 and PPP3CB.
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...
| Publicado en: | Histochemistry & Cell Biology Vol. 145; no. 1; pp. 5 - 17 |
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| Autores principales: | , , , , , , , , |
| Formato: | Journal Article |
| Publicado: |
Springer Nature
Jan2016
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=112234380&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 112234380 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 09486143 NQI jtl: Histochemistry & Cell Biology issn: 09486143 maglogo: N pubinfo: dt: Jan2016 vid: 145 iid: 1 pid: 237 pub: Springer Nature place: New York, New York artinfo: ui: 112234380 10.1007/s00418-015-1368-5 112234380 ppf: 5 ppct: 12 formats: fmt: @attributes: type: P tig: atl: A novel interaction between ATOH8 and PPP3CB. aug: au: Chen, Jingchen Balakrishnan-Renuka, Ajeesh Hagemann, Nina Theiss, Carsten Chankiewitz, Verena Chen, Jinzhong Pu, Qin Erdmann, Kai Brand-Saberi, Beate affil: Department of Anatomy and Molecular Embryology, Medizinische Fakultät, Ruhr-Universität Bochum, Abt. f. Anatomie und Molekulare Embryologie, Geb. MA, 5/158 44780 Bochum Germany sug: ab: 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. pubtype: Academic Journal doctype: Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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