Voltage-dependent calcium channel beta-subunits in combination with alpha 1 subunits, have a GTPase activating effect to promote the hydrolysis of GTP by G alpha o in rat frontal cortex

FEBS Letters
V CampbellA C Dolphin

Abstract

The dihydropyridine-sensitive calcium channel agonist (-)-BayK 8644 was found to produce an enhancement of the intrinsic hydrolysis of GTP by Go in rat frontal cortex membranes. An anti-calcium channel beta-subunit antiserum abolished the (-)-BayK 8644-stimulated hydrolysis of GTP by Go and reduced the dihydropyridine binding capacity of the cortical membranes. A peptide which mimics the beta-subunit binding domain of the calcium channel complex, also attenuated (-)-BayK 8644 activation of GTPase. This study suggests that the calcium channel beta-subunit is the principal component of the channel complex involved in linking dihydropyridine agonist binding to enhanced hydrolysis of GTP by Go. This may be a mechanism by which calcium channels can normally act to limit the duration of a G-protein modulatory signal.

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Citations

May 17, 2005·Pharmacology, Biochemistry, and Behavior·Grazia De LucaGiovambattista De Sarro
Oct 29, 1996·Biochimica Et Biophysica Acta·E J Helmreich, K P Hofmann
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Jul 3, 1999·Physiological Reviews·A MeirR Rahamimoff
Mar 26, 2002·The Journal of Biological Chemistry·Stephen C ParnellJames P Calvet

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