The Journal of General Physiology
Scientifica: Experts in Electrophysiology
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Index of Online Supplemental Material for
J. Gen. Physiol. 10.1085/jgp.200709901
Gonzales-Gutierrez et al.

Figure S1 Deletion of AID domain or point mutation in residue W470 abolishes modulation by CaVβ2a.

Figure S2 CaVβ1b and CaVβ3xo also increase de ratio ionic current charge movement in WT and mutant channels.

Figure S3 Single-channel conductance remains the same in mutant channels.

Figure S4 Single-channel activity for CaV1.2 D469S and CaV1.2 Q473K in the presence of CaVβ2a.

Figure S5 Dwell-time histograms for CaV1.2 D469S and CaV1.2 Q473K in the presence of CaVβ2a.

Figure S6 Burst-duration histograms for CaV1.2 D469S and CaV1.2 Q473K in the presence of CaVβ2a.

Tables S1-S4 (PDF)

 





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