Ines Pankonien

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Ahnak1 has been implicated in protein kinase A (PKA)-mediated control of cardiac L-type Ca(2+) channels (Cav1.2) through its interaction with the Cavβ(2) regulatory channel subunit. Here we corroborate this functional linkage by immunocytochemistry on isolated cardiomyocytes showing co-localization of ahnak1 and Cavβ(2) in the T-tubule system. In previous(More)
Ahnak1, a giant 700 kDa protein, has been implicated in Ca2+ signalling in various cells. Previous work suggested that the interaction between ahnak1 and Cavβ2 subunit plays a role in L-type Ca2+ current (I CaL) regulation. Here, we performed structure–function studies with the most C-terminal domain of ahnak1 (188 amino acids) containing a PxxP consensus(More)
Ahnak1 has been implicated in the beta-adrenergic regulation of the cardiac L-type Ca2+ channel current (I CaL) by its binding to the regulatory Cavβ2 subunit. In this study, we addressed the question whether ahnak1/Cavβ2 interactions are essential or redundant for beta-adrenergic stimulation of I CaL. Three naturally occurring ahnak1 variants (V5075 M,(More)
TMEM16A/anoctamin 1/ANO1 and VRAC/LRRC8 are independent chloride channels activated either by increase in intracellular Ca2+ or cell swelling, respectively. In previous studies, we observed overlapping properties for both types of channels. (i) TMEM16A/ANO1 and LRRC8 are inhibited by identical compounds, (ii) the volume-regulated anion channel VRAC requires(More)
KEY POINTS β-Adrenergic stimulation enhances Ca2+ entry via L-type CaV 1.2 channels, causing stronger contraction of cardiac muscle cells. The signalling pathway involves activation of protein kinase A (PKA), but the molecular details of PKA regulation of CaV 1.2 remain controversial despite extensive research. We show that PKA regulation of CaV 1.2 can be(More)
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