The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.
Structural Basis of Human KCNQ1 Modulation and Gating
Open accessAbstract
Summary KCNQ1, also known as Kv7.1, is a voltage-dependent K+ channel that regulates gastric acid secretion, salt and glucose homeostasis and heart rhythm. Its functional properties are regulated in a tissue-specific manner through co-assembly with beta subunits KCNE1-5. In non-excitable cells KCNQ1 forms a complex with KCNE3, which suppresses channel closure at negative membrane voltages that otherwise would close it. Pore opening is regulated by the signaling lipid PIP2. Using cryo-EM we show that KCNE3 tucks its single membrane spanning helix against KCNQ1, at a location that appears to lock the voltage sensor in its depolarized conformation. Without PIP2, the pore remains closed. Upon addition, PIP2 occupies a site on KCNQ1 within the inner membrane leaflet, which triggers a large conformational change that leads to dilation of the pore’s gate. It is likely that this mechanism of PIP2 activation is conserved among Kv7 channels.
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Metadata
- Authors
- Sun, J., & MacKinnon, R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-01
- Volume
- 180
- Issue
- 2
- Pages
- 340-347.e9
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2997765786
- Cited by
- 293
- References
- 69
- FWCI
- 9.09
- Type
- journal article
- Language
- en
- Open access
- bronze
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