Matches in SemOpenAlex for { <https://semopenalex.org/work/W4319986677> ?p ?o ?g. }
Showing items 1 to 64 of
64
with 100 items per page.
- W4319986677 endingPage "147a" @default.
- W4319986677 startingPage "147a" @default.
- W4319986677 abstract "KATP channels are unique protein complexes of a potassium channel, Kir6.1 or Kir6.2, and an ABC transporter, SUR1, SUR2A or SUR2B (splice variants of SUR2), in a 4:4 stoichiometry. Broadly expressed in many cell types and tissues, KATP channels couple changes in cellular metabolic activity with membrane excitability to control a wide range of physiological processes, including hormone secretion, control of vascular tone, learning and memory, and cardiac and neuronal protection against ischemic insults. In pancreatic β-cells KATP channels formed by Kir6.2 and SUR1 control insulin secretion, and gain- or loss-of-function mutations in these channels cause neonatal diabetes or congenital hyperinsulinism, respectively. Physiological activity of pancreatic KATP channels is regulated by intracellular ATP and ADP. Non-hydrolytic binding of ATP to Kir6.2 inhibits channel activity, while MgATP and MgADP binding to the nucleotide binding domains (NBDs) of SUR1 stimulates channel activity. Besides ATP and ADP, membrane phospholipids in particular PIP2 interacts with Kir6.2 and stimulates channel activity. In addition, pharmacological inhibitors and activators act on SUR1 to modulate channel activity. Although Kir6.2 and SUR1 harbor the primary binding sites for specific physiological and pharmacological ligands, both subunits participate in ligand regulation. How do the potassium channel and the silent ABC transporter work together to decipher signals from different ligands for gating has long been a major question in the KATP channel field. Here, I present structural and functional evidence that SUR1 contributes directly to ATP and PIP2 binding via its TMD0 and L0 linker to enhance Kir6.2 sensitivity to both ligands. Moreover, SUR1 regulates Kir6.2 activity allosterically via its dynamic interaction with the N-terminus of Kir6.2." @default.
- W4319986677 created "2023-02-11" @default.
- W4319986677 creator A5090735854 @default.
- W4319986677 date "2023-02-01" @default.
- W4319986677 modified "2023-09-25" @default.
- W4319986677 title "Untangling the inseparable life of an ABC transporter and a potassium channel: Towards understanding the structure-function relationship in the KATP channel complex" @default.
- W4319986677 doi "https://doi.org/10.1016/j.bpj.2022.11.1022" @default.
- W4319986677 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36782677" @default.
- W4319986677 hasPublicationYear "2023" @default.
- W4319986677 type Work @default.
- W4319986677 citedByCount "0" @default.
- W4319986677 crossrefType "journal-article" @default.
- W4319986677 hasAuthorship W4319986677A5090735854 @default.
- W4319986677 hasConcept C104317684 @default.
- W4319986677 hasConcept C12554922 @default.
- W4319986677 hasConcept C127162648 @default.
- W4319986677 hasConcept C14036430 @default.
- W4319986677 hasConcept C144133560 @default.
- W4319986677 hasConcept C149011108 @default.
- W4319986677 hasConcept C178790620 @default.
- W4319986677 hasConcept C185592680 @default.
- W4319986677 hasConcept C31258907 @default.
- W4319986677 hasConcept C41008148 @default.
- W4319986677 hasConcept C517785266 @default.
- W4319986677 hasConcept C55493867 @default.
- W4319986677 hasConcept C83743174 @default.
- W4319986677 hasConcept C86803240 @default.
- W4319986677 hasConcept C95444343 @default.
- W4319986677 hasConceptScore W4319986677C104317684 @default.
- W4319986677 hasConceptScore W4319986677C12554922 @default.
- W4319986677 hasConceptScore W4319986677C127162648 @default.
- W4319986677 hasConceptScore W4319986677C14036430 @default.
- W4319986677 hasConceptScore W4319986677C144133560 @default.
- W4319986677 hasConceptScore W4319986677C149011108 @default.
- W4319986677 hasConceptScore W4319986677C178790620 @default.
- W4319986677 hasConceptScore W4319986677C185592680 @default.
- W4319986677 hasConceptScore W4319986677C31258907 @default.
- W4319986677 hasConceptScore W4319986677C41008148 @default.
- W4319986677 hasConceptScore W4319986677C517785266 @default.
- W4319986677 hasConceptScore W4319986677C55493867 @default.
- W4319986677 hasConceptScore W4319986677C83743174 @default.
- W4319986677 hasConceptScore W4319986677C86803240 @default.
- W4319986677 hasConceptScore W4319986677C95444343 @default.
- W4319986677 hasIssue "3" @default.
- W4319986677 hasLocation W43199866771 @default.
- W4319986677 hasLocation W43199866772 @default.
- W4319986677 hasOpenAccess W4319986677 @default.
- W4319986677 hasPrimaryLocation W43199866771 @default.
- W4319986677 hasRelatedWork W2019143922 @default.
- W4319986677 hasRelatedWork W2022996845 @default.
- W4319986677 hasRelatedWork W2053671571 @default.
- W4319986677 hasRelatedWork W2083773502 @default.
- W4319986677 hasRelatedWork W2094875452 @default.
- W4319986677 hasRelatedWork W2279134014 @default.
- W4319986677 hasRelatedWork W2357832151 @default.
- W4319986677 hasRelatedWork W2371624924 @default.
- W4319986677 hasRelatedWork W2410438787 @default.
- W4319986677 hasRelatedWork W4240988196 @default.
- W4319986677 hasVolume "122" @default.
- W4319986677 isParatext "false" @default.
- W4319986677 isRetracted "false" @default.
- W4319986677 workType "article" @default.