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Updated: May 16, 2026

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
Published on: December 31, 2013
Transient receptor potential N (TRPN1) from Xenopus interacts with the penta-EF-hand protein peflin
Dominik Wiemuth1, Lena van de Sandt, Rudolf Herr
1Department of Physiology, RWTH Aachen University, 52074 Aachen, Germany.
Abstract:
TRPN1 is a candidate mechanotransduction channel in Drosophila and Caenorhabditis elegans, also present in hair cells of lower vertebrates. At its N-terminal cytoplasmic tail it contains 28 ankyrin repeats. We performed a yeast two-hybrid screen with the N-terminal ankyrin repeats of Xenopus TRPN1 as bait and identified the Penta-EF-hand protein peflin as a putative interaction partner. We confirmed this interaction by GST pulldown assays and by co-localization in an epithelial cell model. Collectively, our study identifies peflin as an interaction partner of TRPN1 in vitro.
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