ArticleThe Journal of general physiology2009
Distinct subdomains of the KCNQ1 S6 segment determine channel modulation by different KCNE subunits.
Article in The Journal of general physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Synergistic effect between the KCNQ1 haplotype and alcohol consumption on the development of type 2 diabetes mellitus in Korean cohorts.Scientific reports · 2021Article
- Control of Biophysical and Pharmacological Properties of Potassium Channels by Ancillary Subunits.Handbook of experimental pharmacology · 2021Article
- Article
- Kv7 Channels in Lung Diseases.Frontiers in physiology · 2020Review
- Functional consequences of a KCNT1 variant associated with status dystonicus and early-onset infantile encephalopathy.Annals of clinical and translational neurology · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Mechanisms Underlying the Dual Effect of Polyunsaturated Fatty Acid Analogs on Kv7.1.Cell reports · 2018Article
- Review
- The C-terminal domain of Kv1.3 regulates functional interactions with the KCNE4 subunit.Journal of cell science · 2016Article
- KCNQ1 subdomains involved in KCNE modulation revealed by an invertebrate KCNQ1 orthologue.The Journal of general physiology · 2011Article
- Voltage-gated potassium channel KCNV2 (Kv8.2) contributes to epilepsy susceptibility.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Allosteric features of KCNQ1 gating revealed by alanine scanning mutagenesis.Biophysical journal · 2011Article
- KCNE4 juxtamembrane region is required for interaction with calmodulin and for functional suppression of KCNQ1.The Journal of biological chemistry · 2011Article
- The membrane protein MiRP3 regulates Kv4.2 channels in a KChIP-dependent manner.The Journal of physiology · 2010Article
- KCNQ1/KCNE1 assembly, co-translation not required.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Modulation of voltage-gated potassium (KV) channels by the KCNE family of single transmembrane proteins has physiological and pathophysiological importance. All five KCNE proteins (KCNE1-KCNE5) have been demonstrated to modulate heterologously expressed KCNQ1 (KV7.1) with diverse effects, making this channel a valuable experimental platform for elucidating structure-function relationships and mechanistic differences among members of this intriguing group of accessory subunits. Here, we specifically investigated the determinants of KCNQ1 inhibition by KCNE4, the least well-studied KCNE protein. In CHO-K1 cells, KCNQ1, but not KCNQ4, is strongly inhibited by coexpression with KCNE4. By studying KCNQ1-KCNQ4 chimeras, we identified two adjacent residues (K326 and T327) within the extracellular end of the KCNQ1 S6 segment that determine inhibition of KCNQ1 by KCNE4. This dipeptide motif is distinct from neighboring S6 sequences that enable modulation by KCNE1 and KCNE3. Conversely, S6 mutations (S338C and F340C) that alter KCNE1 and KCNE3 effects on KCNQ1 do not abrogate KCNE4 inhibition. Further, KCNQ1-KCNQ4 chimeras that exhibited resistance to the inhibitory effects of KCNE4 still interact biochemically with this protein, implying that accessory subunit binding alone is not sufficient for channel modulation. These observations indicate that the diverse functional effects observed for KCNE proteins depend, in part, on structures intrinsic to the pore-forming subunit, and that distinct S6 subdomains determine KCNQ1 responses to KCNE1, KCNE3, and KCNE4.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.