Transmembrane serine protease 2 (TMPRSS2) proteolytically activates the epithelial sodium channel (ENaC) by cleaving the channel’s γ-subunit

Autor: Florian Sure, Marko Bertog, Sara Afonso, Alexei Diakov, Ralf Rinke, M. Gregor Madej, Sabine Wittmann, Thomas Gramberg, Christoph Korbmacher, Alexandr V. Ilyaskin

The epithelial sodium channel (ENaC) is a heterotrimer consisting of α-, β-, and γ-subunits. Channel activation requires proteolytic release of inhibitory tracts from the extracellular domains of α-ENaC and γ-ENaC; however, the proteases involve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1647ad897ede0e49595e59a2dbc68df
https://epub.uni-regensburg.de/52234/

Correction to: Two adjacent phosphorylation sites in the C-terminus of the channel’s α-subunit have opposing effects on epithelial sodium channel (ENaC) activity

Autor: Alexei Diakov, Viatcheslav Nesterov, Anke Dahlmann, Christoph Korbmacher

Publikováno v: Pflügers Archiv - European Journal of Physiology. 474:1037-1037

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5ba6680c4ebea92f9399f450be8d79cf
https://doi.org/10.1007/s00424-022-02717-4

Activation of the Human Epithelial Sodium Channel (ENaC) by Bile Acids Involves the Degenerin Site

Autor: Silke Haerteis, Alexei Diakov, Alexandr V. Ilyaskin, Christoph Korbmacher

Publikováno v: Journal of Biological Chemistry. 291:19835-19847

The epithelial sodium channel (ENaC) is a member of the ENaC/degenerin ion channel family, which also includes the bile acid-sensitive ion channel (BASIC). So far little is known about the effects of bile acids on ENaC function. ENaC is probably a he

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cacb4df1cd9337dcb7930ccd568abe1
https://doi.org/10.1074/jbc.m116.726471

Characterization of the mouse ClC-K1/Barttin chloride channel

Autor: Alexei Diakov, Stéphane Lourdel, Jacques Teulon, Teddy Grand, Olga Andrini, Mathilde Keck, Sébastien L'Hoste, Christoph Korbmacher, Laurent Beck, Laurent Pinelli, Marc Paulais, Mathieu Genete

Publikováno v: Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2013, 1828 (11), pp.2399-2409. ⟨10.1016/j.bbamem.2013.06.012⟩
Biochimica et Biophysica Acta:Biomembranes, 2013, 1828 (11), pp.2399-2409. ⟨10.1016/j.bbamem.2013.06.012⟩

International audience; Several Cl(-) channels have been described in the native renal tubule, but their correspondence with ClC-K1 and ClC-K2 channels (orthologs of human ClC-Ka and ClC-Kb), which play a major role in transcellular Cl(-) absorption

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e4429712cdd2f45cb07305ed601b0a0

A mutation in the β-subunit of ENaC identified in a patient with cystic fibrosis-like symptoms has a gain-of-function effect

Autor: Viatcheslav Nesterov, Christoph Korbmacher, Bettina Krueger, Silke Haerteis, Alexei Diakov, Daniel Soell, Heinrich Sticht, Robert Rauh

Publikováno v: American Journal of Physiology-Lung Cellular and Molecular Physiology. 304:L43-L55

In some patients with atypical cystic fibrosis (CF), only one allele of the CF transmembrane conductance regulator (CFTR) gene is affected. Mutations of the epithelial sodium channel (ENaC) may contribute to the pathophysiology of the disease in thes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::748939a40783f10c2819e02ea03d68e0
https://doi.org/10.1152/ajplung.00093.2012