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  • center
  • program_project
  • nrc
  • whocc
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  • tool
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  • Assistant Professor
  • Associate Professor
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  • Clinical Research Nurse
  • Clinician Researcher
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  • Lab assistant
  • Master Student
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  • Pharmacist
  • PhD Student
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  • Post-doc
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  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
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Scientific Fields
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Published in FEBS Letters - 01 Aug 2017

Amel Bahloul, Elise Pepermans, Bertrand Raynal, Nicolas Wolff, Florence Cordier, Patrick England, Sylvie Nouaille, Bruno Baron, Aziz El-Amraoui, Jean-Pierre Hardelin, Dominique Durand, Christine Petit

Link to Pubmed [PMID] – 28653419

Link to HAL – pasteur-01858477

Link to DOI – 10.1002/1873-3468.12729

FEBS Letters, 2017, 591 (15), pp.2299 - 2310. ⟨10.1002/1873-3468.12729⟩

Mutations in the gene encoding harmonin, a multi-PDZ domain-containing submembrane protein, cause Usher syndrome type 1 (congenital deafness and balance disorder, and early-onset sight loss). The structure of the protein and biological activities of its three different classes of splice isoforms (a, b, and c) remain poorly understood. Combining biochemical and biophysical analyses , we show that harmonin-a1 can switch between open and closed conforma-tions through intramolecular binding of its C-terminal PDZ-binding motif to its N-terminal supramodule NTD-PDZ1 and through a flexible PDZ2-PDZ3 linker. This conformational switch presumably extends to most harmonin iso-forms, and it is expected to have an impact on the interaction with some binding partners, as shown here for cadherin-related 23, another component of the hair cell mechanoelectrical transduction machinery.