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  Native Piezo2 interactomics identifies pericentrin as a novel regulator of Piezo2 in somatosensory neurons.

Narayanan, P., Sondermann, J., Rouwette, T., Karaca, S., Urlaub, H., Mitkovski, M., et al. (2016). Native Piezo2 interactomics identifies pericentrin as a novel regulator of Piezo2 in somatosensory neurons. Journal of Proteome Research, 15(8), 2676-2687. doi:10.1021/acs.jproteome.6b00235.

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 Urheber:
Narayanan, P., Autor
Sondermann, J., Autor
Rouwette, T., Autor
Karaca, S.1, Autor           
Urlaub, H.1, Autor           
Mitkovski, M., Autor
Gomez-Varela, D., Autor
Schmidt, M., Autor
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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Schlagwörter: Interactomics; Piezo2; Quantitative mass spectrometry; Rapidly adapting mechanically activated currents; Vertebrate mechanotransduction
 Zusammenfassung: The ability of somatosensory neurons to perceive mechanical stimuli relies on specialized mechanotransducing proteins and their molecular environment. Only recently has the identity of a major transducer of mechanical forces in vertebrates been revealed by the discovery of Piezo2. Further work has established its pivotal role for innocuous touch in mice. Therefore, Piezo2 offers a unique platform for the molecular investigation of somatosensory mechanosensation. We performed a mass spectrometry-based interactomics screen on native Piezo2 in somatosensory neurons of mouse dorsal root ganglia (DRG). Stringent and quantitative data analysis yielded the identity of 36 novel binding partners of Piezo2. The biological significance of this data set is reflected by functional experiments demonstrating a role for Pericentrin in modulating Piezo2 activity and membrane expression in somatosensory neurons. Collectively, our findings provide a framework for understanding Piezo2 physiology and serve as a rich resource for the molecular dissection of mouse somatosensation.

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Sprache(n): eng - English
 Datum: 2016-06-262016-08-05
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1021/acs.jproteome.6b00235
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Titel: Journal of Proteome Research
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 15 (8) Artikelnummer: - Start- / Endseite: 2676 - 2687 Identifikator: -