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Molecular mechanisms and physiological relevance of RGK proteins in the heart
Author(s) -
Meza U.,
Beqollari D.,
Bannister R. A.
Publication year - 2018
Publication title -
acta physiologica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.591
H-Index - 116
eISSN - 1748-1716
pISSN - 1748-1708
DOI - 10.1111/apha.13016
Subject(s) - gene isoform , cav1.2 , myocyte , microbiology and biotechnology , biology , cardiovascular physiology , cardiac function curve , hek 293 cells , chemistry , medicine , endocrinology , biochemistry , protein subunit , receptor , gene , heart failure
Abstract The primary route of Ca 2+ entry into cardiac myocytes is via 1,4‐dihydropyridine‐sensitive, voltage‐gated L‐type Ca 2+ channels. Ca 2+ influx through these channels influences duration of action potential and engages excitation‐contraction ( EC ) coupling in both the atria and the myocardium. Members of the RGK (Rad, Rem, Rem2 and Gem/Kir) family of small GTP ‐binding proteins are potent, endogenously expressed inhibitors of cardiac L‐type channels. Although much work has focused on the molecular mechanisms by which RGK proteins inhibit the Ca V 1.2 and Ca V 1.3 L‐type channel isoforms that expressed in the heart, their impact on greater cardiac function is only beginning to come into focus. In this review, we summarize recent findings regarding the influence of RGK proteins on normal cardiac physiology and the pathological consequences of aberrant RGK activity.