Regulation of Ca2+ channel expression at the cell surface by the small G-protein kir/Gem

Pascal Béguin, Kazuaki Nagashima, Tohru Gonoi, Tadao Shibasaki, Kazuo Takahashi, Yasushige Kashima, Nobuaki Ozaki, Käthi Geering, Toshihiko Iwanaga and Susumu Seino ()
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Pascal Béguin: Graduate School of Medicine, Chiba University
Kazuaki Nagashima: Graduate School of Medicine, Chiba University
Tohru Gonoi: Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, 1-8-1
Tadao Shibasaki: Graduate School of Medicine, Chiba University
Kazuo Takahashi: Core Research for Evolutional Science and Technology (CREST), Graduate School of Medicine, Chiba University
Yasushige Kashima: Graduate School of Medicine, Chiba University
Nobuaki Ozaki: Graduate School of Medicine, Chiba University
Käthi Geering: Institut de Pharmacologie et de Toxicologie de l'Université de Lausanne
Toshihiko Iwanaga: Laboratory of Anatomy, Graduate School of Veterinary Medicine, Hokkaido University
Susumu Seino: Graduate School of Medicine, Chiba University

Nature, 2001, vol. 411, issue 6838, 701-706

Abstract: Abstract Voltage-dependent calcium (Ca2+) channels are involved in many specialized cellular functions1,2,3, and are controlled by intracellular signals such as heterotrimeric G-proteins4, protein kinases5,6 and calmodulin (CaM)7,8. However, the direct role of small G-proteins in the regulation of Ca2+ channels is unclear. We report here that the GTP-bound form of kir/Gem, identified originally as a Ras-related small G-protein that binds CaM9,10,11, inhibits high-voltage-activated Ca2+ channel activities by interacting directly with the β-subunit. The reduced channel activities are due to a decrease in α1-subunit expression at the plasma membrane. The binding of Ca2+/CaM to kir/Gem is required for this inhibitory effect by promoting the cytoplasmic localization of kir/Gem. Inhibition of L-type Ca2+ channels by kir/Gem prevents Ca2+-triggered exocytosis in hormone-secreting cells. We propose that the small G-protein kir/Gem, interacting with β-subunits, regulates Ca2+ channel expression at the cell surface.

Date: 2001
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DOI: 10.1038/35079621

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