Functional assessment of three Rem residues identified as critical for interactions with Ca(2+) channel β subunits

Pflügers Archiv : European journal of physiology
D BeqollariR A Bannister

Abstract

Members of the Rem, Rem2, Rad, Gem/Kir (RGK) family of small GTP-binding proteins inhibit high-voltage-activated (HVA) Ca(2+) channels through interactions with both the principal α1 and the auxiliary β subunits of the channel complex. Three highly conserved residues of Rem (R200, L227, and H229) have been shown in vitro to be critical for interactions with β subunits. However, the functional significance of these residues is not known. To investigate the contributions of R200, L227, and H229 to β subunit-mediated RGK protein-dependent inhibition of HVA channels, we introduced alanine substitutions into all three positions of Venus fluorescent protein-tagged Rem (V-Rem AAA) and made three other V-Rem constructs with an alanine introduced at only one position (V-Rem R200A, V-Rem L227A, and V-Rem H229A). Confocal imaging and immunoblotting demonstrated that each Venus-Rem mutant construct had comparable expression levels to Venus-wild-type Rem when heterologously expressed in tsA201 cells. In electrophysiological experiments, V-Rem AAA failed to inhibit N-type Ca(2+) currents in tsA201 cells coexpressing CaV2.2 α1B, β3, and α2δ-1 channel subunits. The V-Rem L227A single mutant also failed to reduce N-type currents conducted by co...Continue Reading

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Citations

Jun 17, 2015·The Journal of General Physiology·Donald BeqollariRoger A Bannister
Apr 25, 2019·The Journal of General Physiology·Sidharth TyagiRoger A Bannister
Jan 13, 2018·The Journal of Biological Chemistry·Donald BeqollariRoger A Bannister
Nov 7, 2018·Proceedings of the National Academy of Sciences of the United States of America·Akil A PuckerinHenry M Colecraft
Jul 15, 2021·Cell Calcium·Daniel R MirandaRoger A Bannister

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