Talbi, Khaoula and Ousingsawat, Jiraporn and Centeio, Raquel and Schreiber, Rainer and Kunzelmann, Karl (2023) KCNE1 does not shift TMEM16A from a Ca²⁺ dependent to a voltage dependent Cl⁻ channel and is not expressed in renal proximal tubule. PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 475 (8). pp. 995-1007. ISSN 0031-6768, 1432-2013
Full text not available from this repository. (Request a copy)Abstract
The TMEM16A (ANO1) Cl- channel is activated by Ca2+ in a voltage-dependent manner. It is broadly expressed and was shown to be also present in renal proximal tubule (RPT). KCNQ1 is an entirely different K+ selective channel that forms the cardiac I-KS potassium channel together with its ss-subunit KCNE1. Surprisingly, KCNE1 has been claimed to interact with TMEM16A, and to be required for activation of TMEM16A in mouse RPT. Interaction with KCNE1 was reported to switch TMEM16A from a Ca2(2+)-dependent to a voltage-dependent ion channel. Here we demonstrate that KCNE1 is not expressed in mouse RPT. TMEM16A expressed in RPT is activated by angiotensin II and ATP in a KCNE1-independent manner. Coexpression of KCNE1 does not change TMEM16A to a voltage gated Cl- channel and Ca2+-dependent regulation of TMEM16A is fully maintained in the presence of KCNE1. While overexpressed KCNE1 slightly affects Ca2+-dependent regulation of TMEM16A, the data provide no evidence for KCNE1 being an auxiliary functional subunit for TMEM16A.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CALCIUM; FORM; ISK; K+; K(V)LQT1; PROTEINS; TMEM16A; KCNE1; KCNQ1; Channel regulation; Voltage dependence; Ca2+ activated Cl- channel |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Physiologie > Prof. Dr. Karl Kunzelmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 01 Mar 2024 07:03 |
| Last Modified: | 01 Mar 2024 07:03 |
| URI: | https://pred.uni-regensburg.de/id/eprint/59230 |
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