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A novel interaction between ATOH8 and PPP3CB.

Jingchen Chen1,2, Ajeesh Balakrishnan-Renuka1, Nina Hagemann3

  • 1Department of Anatomy and Molecular Embryology, Medizinische Fakultät, Ruhr-Universität Bochum, Abt. f. Anatomie und Molekulare Embryologie, Geb. MA, 5/158, 44780, Bochum, Germany.

Histochemistry and Cell Biology
|October 27, 2015
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Summary
This summary is machine-generated.

The transcription factor ATOH8 interacts with PPP3CB, a calcineurin subunit. This interaction is crucial for ATOH8

Keywords:
ATOH8CalcineurinCyclosporin APPP3CB

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Developmental Biology

Background:

  • ATOH8 is a bHLH transcription factor involved in diverse developmental processes.
  • PPP3CB is the catalytic subunit of calcineurin, a serine/threonine phosphatase regulating protein activity.
  • Calcineurin's role in cellular processes necessitates understanding its interaction partners.

Purpose of the Study:

  • To investigate the interaction between ATOH8 and PPP3CB.
  • To identify the domains involved in the ATOH8-PPP3CB interaction.
  • To determine the functional consequence of this interaction on ATOH8 localization and activity.

Main Methods:

  • In vitro interaction assays to confirm binding between ATOH8 and PPP3CB.
  • Domain mapping to pinpoint interacting regions on both proteins.
  • Treatment with calcineurin inhibitor cyclosporin A (CsA) to assess functional impact.

Main Results:

  • ATOH8 directly interacts with PPP3CB in vitro.
  • The catalytic domain of PPP3CB interacts with both the N-terminus and bHLH domain of ATOH8.
  • ATOH8 selectively binds PPP3CB over PPP3CA, likely due to PPP3CB's unique N-terminal proline-rich region.
  • Inhibition of the interaction with CsA causes ATOH8 to remain in the cytoplasm.

Conclusions:

  • The interaction between ATOH8 and PPP3CB is specific and mediated by distinct protein domains.
  • This interaction is essential for the nuclear localization of ATOH8, which is critical for its function as a transcription factor.
  • Understanding this interaction provides insights into the regulation of developmental processes involving ATOH8.