IndraLab

Statements


| 4

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"Formation of the maxi-K and caveolin complex may involve redundant pathways, thus making it difficult to completely disrupt this complex."

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"Given that the physical formation of the maxi-K and caveolin complex may be insufficient to regulate all maxi-K channel activity, a second mechanism involving only the 1007 YNMLCFGIY 1015 motif may contribute to the ability of cav-1 to activate the maxi-K-generated current."

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"Interestingly, all three of the mutants used in this study reproduced the inhibitory effects of cav-1 deficiency on maxi-K channel current in hMSMCs, although only in the case of mutant Y1007A, F1012A, Y1015A was the maxi-K and caveolin complex disrupted."

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"Slo1 caveolin binding motif, a mechanism of caveolin-1-Slo1 interaction regulating Slo1 surface expression."