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Since PY motifs are known ligands to WW domains, we investigated their role for H1 regulation and the possible involvement of the WW domain containing ubiquitin\u2010protein ligase Nedd4, taking advantage of the <jats:italic>Xenopus<\/jats:italic> oocyte system. Mutation of the PY motif leads to higher peak currents when compared to wild\u2010type channel. Moreover, co\u2010expression of Nedd4 reduced the peak currents, whereas an enzymatically inactive Nedd4 mutant increased them, likely by competing with endogenous Nedd4. The effect of Nedd4 was not observed in the PY motif mutated channel or in the skeletal muscle voltage\u2010gated Na<jats:sup>+<\/jats:sup> channel, which lacks a PY motif. We conclude that H1 may be regulated by Nedd4 depending on WW\u2013PY interaction, and on an active ubiquitination site.<\/jats:p>","DOI":"10.1016\/s0014-5793(00)01098-x","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T17:52:27Z","timestamp":1027619547000},"page":"377-380","source":"Crossref","is-referenced-by-count":89,"title":["Regulation of the cardiac voltage\u2010gated Na<sup>+<\/sup> channel (H1) by the ubiquitin\u2010protein ligase Nedd4"],"prefix":"10.1002","volume":"466","author":[{"given":"Hugues","family":"Abriel","sequence":"first","affiliation":[]},{"given":"Elena","family":"Kamynina","sequence":"additional","affiliation":[]},{"given":"Jean-Daniel","family":"Horisberger","sequence":"additional","affiliation":[]},{"given":"Olivier","family":"Staub","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2000,1,25]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.1992.72.suppl_4.S15"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1469-7793.1998.647bp.x"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1161\/01.RES.83.4.441"},{"key":"e_1_2_6_5_1","first-page":"604","volume":"39","author":"White M.M.","year":"1991","journal-title":"Mol. 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