Lipid regulation of BK channel function

Research output: Contribution to journalShort survey

22 Citations (Scopus)

Abstract

This mini-review focuses on lipid modulation of BK (MaxiK, BKCa) current by a direct interaction between lipid and the BK subunits and/or their immediate lipid environment. Direct lipid-BK protein interactions have been proposed for fatty and epoxyeicosatrienoic acids, phosphoinositides and cholesterol, evidence for such action being less clear for other lipids. BK α (slo1) subunits are sufficient to support current perturbation by fatty and epoxyeicosatrienoic acids, glycerophospholipids and cholesterol, while distinct BK β subunits seem necessary for current modulation by most steroids. Subunit domains or amino acids that participate in lipid action have been identified in a few cases: hslo1 Y318, cerebral artery smooth muscle (cbv1) R334,K335,K336, cbv1 seven cytosolic CRAC domains, slo1 STREX and β1 T169,L172,L173 for docosahexaenoic acid, PIP2, cholesterol, sulfatides, and cholane steroids, respectively. Whether these protein motifs directly bind lipids or rather transmit the energy of lipid binding to other areas and trigger protein conformation change remains unresolved. The impact of direct lipid-BK interaction on physiology is briefly discussed.

Original languageEnglish (US)
Article numberArticle 312
JournalFrontiers in Physiology
Volume5 AUG
DOIs
StatePublished - Jan 1 2014

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Large-Conductance Calcium-Activated Potassium Channels
Lipids
Cholanes
Fatty Acids
Steroids
Cholesterol
Trigger Points
Glycerophospholipids
Amino Acid Motifs
Protein Conformation
Cerebral Arteries
Docosahexaenoic Acids
Phosphatidylinositols
Smooth Muscle
Amino Acids

All Science Journal Classification (ASJC) codes

  • Physiology
  • Physiology (medical)

Cite this

Lipid regulation of BK channel function. / Dopico, Alejandro; Bukiya, Anna.

In: Frontiers in Physiology, Vol. 5 AUG, Article 312, 01.01.2014.

Research output: Contribution to journalShort survey

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