IndraLab

"Remarkably, colabeling experiments revealed that beta2 co-transfection induced a large proportion of hSlo (green) to appear clearly punctuated (E, F) resembling the beta2 (red) expression pattern (G, [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"Similarly, data from a previous study suggest that the dual gating mechanisms also underlie beta2 modulation of BK channel properties."

"This also explains why beta2 does not potentiate BK channel gating at 0 Ca 2+."

"In cell attached recordings, the beta 2 -selective agonist salbutamol increased BK channel activity largely only if both the beta 2 AR and the AKAP-150 homolog AKAP79 were coexpressed in Xenopus oocytes."

"This new mode of beta2 modulation of hSlo may depend on particular coregulatory mechanisms in different cell types."

"Inactivation of I (transient) could be removed by extracellular papain and could later be restored by intracellular application of the ' ball ' domain of the auxiliary subunit (beta2) thought to mediate BK channel inactivation in rat chromaffin cells."

"For example, beta4 makes channels resistant to iberiotoxin blockade [XREF_BIBR], gamma1 (also named LRRC26) makes channels resistant to mallotoxin activation [XREF_BIBR], beta2 produces MaxiK channels that inactivate with time [XREF_BIBR], beta3b produces channels with very fast inactivation producing currents that appear to activate fast and rectify [XREF_BIBR, XREF_BIBR], beta1 increases Ca 2+ / voltage sensitivity when free Ca 2+ facing the inside of the channel is beyond 1 muM [XREF_BIBR], while gamma1-gamma4 produce channels with increased voltage sensitivity even without Ca 2+ [XREF_BIBR, XREF_BIBR]."

"The new data indicates that LTCC currents are also required for daytime beta2 mediated BK channel inactivation, possibly because beta2 adjusts BK calcium sensitivity, or somehow promotes BK association with LTCC."

"For example, the gamma1 subunit (LRRC26) and beta1 subunit shift the V 50 of Slo1 by over 100 mV XREF_BIBR, XREF_BIBR, and the beta2 and beta3 subunits cause great inactivation of Slo1 XREF_BIBR, XREF_BIBR."