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Isolation and Characterization of Connexin26 Gap Junctions from Transfected Hela Cells

Published online by Cambridge University Press:  02 July 2020

G. Hand ,
V. Nguyen ,
K. Downing ,
D. Mueller ,
A. Engel ,
Bruce Nicholson  and
G. Sosinsky
G. Hand
Affiliation:
University of California, San Diego, La Jolla, CA92093-0505;
V. Nguyen
Affiliation:
University of California, San Diego, La Jolla, CA92093-0505;
K. Downing
Affiliation:
Donner Lab, Lawrence Berkeley Laboratory, BerkeleyCA9472
D. Mueller
Affiliation:
M.E.Mueller Institute for Structural Biology, Biozentrum, Basel, Switzerland and State University of New York at Buffalo, Buffalo, NY 14260
A. Engel
Affiliation:
M.E.Mueller Institute for Structural Biology, Biozentrum, Basel, Switzerland and State University of New York at Buffalo, Buffalo, NY 14260
Bruce Nicholson
Affiliation:
State University of New York at Buffalo, Buffalo, NY 14260
G. Sosinsky
Affiliation:
University of California, San Diego, La Jolla, CA92093-0505;
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Extract

Gap junctions are composed of a multigene family of proteins called the connexins with a similar sequence and folding topology. Connexons, half-channels made from a particular connexin, will dock and form functional channels with some, but not all, connexons made of other isoforms. This is surprising considering that the primary sequences of the docking domains are conserved and in some cases there are limited amino acid changes in the extracellular loops between compatible connexins. Therefore, some tertiary or quaternary interactions between the extracellular loops of the two docking hemichannels must contribute to the compatibility of a connexon assembled from one connexin for a connexon made from a different connexin. The 3D structures of gap junctions composed of only three isoforms have been investigated with only one case of a gap junction structure at better than 1 nm resolution [1]. The rat liver hemichannel structure is the only one that contains an exposed extracellular surface [2].

Type
Electron Cryomicroscopy of Macromolecules
Information
Microscopy and Microanalysis , Volume 6 , Issue S2: Proceedings: Microscopy & Microanalysis 2000, Microscopy Society of America 58th Annual Meeting, Microbeam Analysis Society 34th Annual Meeting, Microscopical Society of Canada/Societe de Microscopie de Canada 27th Annual Meeting, Philadelphia, Pennsylvania August 13-17, 2000 , August 2000 , pp. 246 - 247
Copyright
Copyright © Microscopy Society of America

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References

[1]Unger, V.M., Kumar, N.M., Gilula, N.B. and Yeager, M. (1999) Science 283: 1176–1180.CrossRefGoogle Scholar
[2]Perkins, G.A., Goodenough, D.A. and Sosinsky, G.E. (1997) Biophys. J. 72: 533–544.CrossRefGoogle Scholar
[3]Fallon, R.F. and Goodenough, D.A. (1981) J. Cell Biol. 90: 521–526.CrossRefGoogle Scholar
[4]Elfgang, C, Eckert, R., Lichtenberg-Fraté, H., Butterweck, A., Traub, O., Klein, R.A., Hülser, D.F. and Willecke, K. (1995) J. Cell Biol. 129:805–817.CrossRefGoogle Scholar
[5]Hülser, D.F., Rehkopf, B. and Traub, O. (1997) Exp. Cell Res. 233: 240–251.CrossRefGoogle Scholar
[6]Hoh, J., G. E., Sosinsky, J.-P., Revel, and P. K., Hansma. 1993. Biophys. J. 65:149–163.CrossRefGoogle Scholar
[7] Funded by NSF MCB-9728338, N1H grants RR04050, CA48049, and GM48773Google Scholar