Gewählte Publikation:
Kepplinger, KJ; Kahr, H; Förstner, G; Sonnleitner, M; Schindler, H; Schmidt, T; Groschner, K; Soldatov, NM; Romanin, C.
A sequence in the carboxy-terminus of the alpha(1C) subunit important for targeting, conductance and open probability of L-type Ca(2+) channels.
FEBS Lett. 2000; 477(3):161-169
Doi: 10.1016/S0014-5793(00)01791-9
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- Co-Autor*innen der Med Uni Graz
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Groschner Klaus
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- Abstract:
- The role of the 80-amino acid motif 1572-1651 in the C-terminal tail of alpha(1C) Ca(2+) channel subunits was studied by comparing properties of the conventional alpha(1C,77) channel expressed in HEK-tsA201 cells to three isoforms carrying alterations in this motif. Replacement of amino acids 1572-1651 in alpha(1C,77) with 81 non-identical residues leading to alpha(1C,86) impaired membrane targeting and cluster formation of the channel. Similar to alpha(1C, 86), substitution of its 1572-1598 (alpha(1C,77L)) or 1595-1652 (alpha(1C,77K)) segments into the alpha(1C,77) channel yielded single-channel Ba(2+) currents with increased inactivation, reduced open probability and unitary conductance, when compared to the alpha(1C,77) channel. Thus, the C-terminal sequence 1572-1651 of the alpha(1C) subunit is important for membrane targeting, permeation and open probability of L-type Ca(2+) channels.
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Amino Acid Sequence -
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Calcium Channels, L-Type - chemistry Calcium Channels, L-Type - physiology
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Cell Line -
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Humans -
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Ion Channel Gating -
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Membrane Potentials -
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Molecular Sequence Data -
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Probability -
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Protein Isoforms - chemistry Protein Isoforms - physiology
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Recombinant Proteins - chemistry Recombinant Proteins - metabolism
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Subcellular Fractions - metabolism
- Find related publications in this database (Keywords)
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class C-type Ca2+ channel
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carboxyl tail
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targeting
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conductance
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inactivation
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fluorescence microscopy
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GFP-labeled alpha(1C) subunit