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- W2185978952 abstract "Large conductance, calcium-activated K (BK) channels are important regulators of cell excitability and recognized targets of intracellular kinases. BK channel modulation by tyrosine kinases, including focal adhesion kinase and c-src, suggests their potential involvement in integrin signaling. Recently, we found that fibronectin, an endogenous 51 integrin ligand, enhances BK channel current through both Ca 2 - and phosphorylation-dependent mechanisms in vascular smooth muscle. Here, we show that macroscopic currents from HEK 293 cells expressing murine BK channel -subunits (mSlo) are acutely potentiated following 51 integrin activation. The effect occurs in a Ca 2 -dependent manner, 1–3 min after integrin engagement. After integrin activation, normalized conductance-voltage relations for mSlo are leftshifted at free Ca 2 concentrations >1 M. Overexpression of human c-src with mSlo, in the absence of integrin activation, leads to similar shifts in mSlo Ca 2 sensitivity, whereas overexpression of catalytically inactive c-src blocks integrin-induced potentiation. However, neither integrin activation nor c-src overexpression potentiates current in BK channels containing a point mutation at Tyr-766. Biochemical tests confirmed the critical importance of residue Tyr-766 in integrin-induced channel phosphorylation. Thus, BK channel activity is enhanced by51 integrin activation, likely through an intracellular signaling pathway involving c-src phosphorylation of the channel -subunit at Tyr-766. The net result is increased current amplitude, enhanced Ca 2 sensitivity," @default.
- W2185978952 created "2016-06-24" @default.
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- W2185978952 date "2010-01-01" @default.
- W2185978952 modified "2023-09-27" @default.
- W2185978952 title "51 Integrin Engagement Increases Large Conductance, Ca 2 -activatedKChannelCurrentandCa 2 Sensitivity" @default.
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