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Published 14 August 2006. doi:10.1083/jcb.200601115
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 4, 535-546
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Article

 Functional implications of calcium permeability of the channel formed by pannexin 1

Fabien Vanden Abeele, Gabriel Bidaux, Dmitri Gordienko, Benjamin Beck, Yuri V. Panchin, Ancha V. Baranova, Dmitry V. Ivanov, Roman Skryma, and Natalia Prevarskaya

Institut National de la Santé et de la Recherche Médicale, U800, Equipe labellisée par la Ligue Contre le Cancer, Universite des Sciences et Technologies de Lille, Villeneuve d'Ascq Cedex, F-59655 France

Correspondence to Natalia Prevarskaya: natacha.prevarskaya{at}univ-lille1.fr

Although human pannexins (PanX) are homologous to gap junction molecules, their physiological function in vertebrates remains poorly understood. Our results demonstrate that overexpression of PanX1 results in the formation of Ca2+-permeable gap junction channels between adjacent cells, thus, allowing direct intercellular Ca2+ diffusion and facilitating intercellular Ca2+ wave propagation. More intriguingly, our results strongly suggest that PanX1 may also form Ca2+-permeable channels in the endoplasmic reticulum (ER). These channels contribute to the ER Ca2+ leak and thereby affect the ER Ca2+ load. Because leakage remains the most enigmatic of those processes involved in intracellular calcium homeostasis, and the molecular nature of the leak channels is as yet unknown, the results of this work provide new insight into calcium signaling mechanisms. These results imply that for vertebrates, a new protein family, referred to as pannexins, may not simply duplicate the connexin function but may also provide additional pathways for intra- and intercellular calcium signaling and homeostasis.

F. Vanden Abeele, G. Bidaux, and D. Gordienko contributed equally to this paper.

Y.V. Panchin's present addresses are Institute for Information Transmission Problems, Russian Academy of Sciences, Moscow 101447, Russia; and the A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia.

D.V. Ivanov's present address is Dept. of Ophthalmology, Bascom Palmer Eye Institute, University of Miami Miller School of Medicine, Miami, FL 33136.

D. Gordienko's present address is Dept. of Basic Medical Sciences, St. George's University of London, London SW17 0RE, England, UK.

A.V. Baranova's present addresses are Dept. of Molecular and Microbiology, Georges Mason University, Manassas, VA 20110; and the Russian Academy of Medical Science, 123098 Moscow, Russia.

Abbreviations used in this paper: BODIPY, boron dipyrromethene difluoride; HEK, human embryonic kidney; ODN, oligodeoxynucleotide; RyR, ryanodine receptor; SERCA, sarcoplasmic/ER Ca2+-ATPase; TG, thapsigargin.


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