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Volume 271, Number 48, Issue of November 29, 1996 pp. 30330-30335
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Two Amino Acid Residues in the IIIS5 Segment of L-Type Calcium Channels Differentially Contribute to 1,4-Dihydropyridine Sensitivity

(Received for publication, July 24, 1996)

Jörg Mitterdorfer , Zhengyi Wang , Martina J. Sinnegger , Steffen Hering , Jörg Striessnig , Manfred Grabner and Hartmut Glossmann

From the Institut für Biochemische Pharmakologie, Peter Mayr Strasse 1, A-6020 Innsbruck, Austria

The transmembrane segment IIIS5 of the L-type calcium channel alpha 1 subunit participates in the formation of the 1,4-dihydropyridine (DHP) interaction domain (Grabner, M., Wang, Z., Hering, S., Striessnig, J., and Glossmann, H. (1996) Neuron 16, 207-218). We applied mutational analysis to identify amino acid residues within this segment that contribute to DHP sensitivity. DHP agonist and antagonist modulation of Ba2+ inward currents was assessed after coexpression of chimeric and mutant calcium channel alpha 1 subunits with alpha 2delta and beta 1a subunits in Xenopus oocytes. Whereas DHP antagonists required Thr-1066, DHP agonist modulation crucially depended on the additional presence of Gln-1070 (numbering according to alpha 1C-a), which also further increased the sensitivity to DHP antagonists. Asp-955, which is found at the corresponding position in the calcium channel alpha 1S subunit from carp skeletal muscle, displayed functional similarity to Gln-1070 with respect to DHP interaction. We conclude that these residues (Thr-1066 plus Gln-1070 or Asp-955), which are located in close vicinity on the same side of the putative alpha -helix of transmembrane segment IIIS5, form a crucial DHP binding motif.


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