The second transmembrane domain of the large conductance, voltage- and calcium-gated potassium channel β1 subunit is a lithocholate sensor

Anna Bukiya, Thirumalini Vaithianathan, Ligia Toro, Alejandro Dopico

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Bile acids and other steroids modify large conductance, calcium- and voltage-gated potassium (BK) channel activity contributing to non-genomic modulation of myogenic tone. Accessory BK β1 subunits are necessary for lithocholate (LC) to activate BK channels and vasodilate. The protein regions that sense steroid action, however, remain unknown. Using recombinant channels in 1-palmitoyl-2-oleoyl-phosphatidylethanolamine/1-palmitoyl-2-oleoyl-phosphatidylserine bilayers we now demonstrate that complex proteolipid domains and cytoarchitecture are unnecessary for β1 to mediate LC action; β1 and a simple phospholipid microenvironment suffice. Since β1 senses LC but β4 does not, we made chimeras swapping regions between these subunits and, following channel heterologous expression, demonstrate that β1 TM2 is a bile acid-recognizing sensor.

Original languageEnglish (US)
Pages (from-to)673-678
Number of pages6
JournalFEBS Letters
Volume582
Issue number5
DOIs
StatePublished - Mar 5 2008

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Lithocholic Acid
Voltage-Gated Potassium Channels
Potassium Channels
Large-Conductance Calcium-Activated Potassium Channels
Calcium
Bile Acids and Salts
Sensors
Electric potential
Steroids
Proteolipids
Phosphatidylserines
Accessories
Phospholipids
Potassium
Modulation
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The second transmembrane domain of the large conductance, voltage- and calcium-gated potassium channel β1 subunit is a lithocholate sensor. / Bukiya, Anna; Vaithianathan, Thirumalini; Toro, Ligia; Dopico, Alejandro.

In: FEBS Letters, Vol. 582, No. 5, 05.03.2008, p. 673-678.

Research output: Contribution to journalArticle

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