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<p>Large conductance voltage- and Ca<sup>2</sup>⁺-activated K⁺ (BK) channels are key regulators of membrane excitability and intracellular Ca<sup>2</sup>⁺ signaling in a wide range of excitable and non-excitable cells. Although the biophysical properties of BK channels have been extensively characterized, it has become increasingly clear that their functional diversity arises largely from interactions with a broad network of associated proteins. In this focused review, we provide an updated overview of the BK channel protein interactome, highlighting how these interactions shape channel gating, trafficking, localization, and coupling to Ca<sup>2</sup>⁺ sources. We discuss well-established regulatory partners, including β and γ auxiliary subunits, as well as emerging modulators such as BKIP-1 and LINGO-1. We further examine interactions with cytoskeletal and trafficking proteins that govern BK channel surface expression and mobility, and with Ca<sup>2</sup>⁺-permeable channels and receptors, including voltage-gated Ca<sup>2</sup>⁺ channels, TRP channels, ryanodine receptors, IP₃ receptors, and NMDA receptors, that create specialized Ca<sup>2</sup>⁺ signaling nanodomains. Finally, we summarize the roles of intracellular signaling molecules and scaffolding proteins that integrate BK channels into larger signaling assemblies. Together, these findings position BK channels as central hubs within multiprotein complexes that enable precise, context-dependent control of cellular excitability and Ca<sup>2</sup>⁺-dependent physiological processes.</p>

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The BK channel interactome: molecular partnerships and biophysical implications

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月20日

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  • Nadya Yanes-Alonso,
  • Bárbara Armas-Rijo,
  • Andrea Reyes-Carrión,
  • Rebeca Navarro-Alonso,
  • Luis O. Romero,
  • David Bartolomé-Martín,
  • Teresa Giraldez

摘要

Large conductance voltage- and Ca2⁺-activated K⁺ (BK) channels are key regulators of membrane excitability and intracellular Ca2⁺ signaling in a wide range of excitable and non-excitable cells. Although the biophysical properties of BK channels have been extensively characterized, it has become increasingly clear that their functional diversity arises largely from interactions with a broad network of associated proteins. In this focused review, we provide an updated overview of the BK channel protein interactome, highlighting how these interactions shape channel gating, trafficking, localization, and coupling to Ca2⁺ sources. We discuss well-established regulatory partners, including β and γ auxiliary subunits, as well as emerging modulators such as BKIP-1 and LINGO-1. We further examine interactions with cytoskeletal and trafficking proteins that govern BK channel surface expression and mobility, and with Ca2⁺-permeable channels and receptors, including voltage-gated Ca2⁺ channels, TRP channels, ryanodine receptors, IP₃ receptors, and NMDA receptors, that create specialized Ca2⁺ signaling nanodomains. Finally, we summarize the roles of intracellular signaling molecules and scaffolding proteins that integrate BK channels into larger signaling assemblies. Together, these findings position BK channels as central hubs within multiprotein complexes that enable precise, context-dependent control of cellular excitability and Ca2⁺-dependent physiological processes.