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Three-Dimensional Cellular Organization of Gap Junction Connexins Revealed by Specific Labeling and Electron Tomography

Published online by Cambridge University Press:  02 July 2020

G. Sosinsky ,
G. Hand ,
G. Gaietta ,
T. Deerinck ,
M. Martone ,
S. Adams ,
A. Stelljes ,
K. Jordan ,
D. W. Laird  and
R. Tsien
...Show all authors
G. Sosinsky
Affiliation:
National Center for Microscopy and Imaging Research, Dept. of Neurosciences University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093. The San Diego Supercomputer Center University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
G. Hand
Affiliation:
National Center for Microscopy and Imaging Research, Dept. of Neurosciences University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
G. Gaietta
Affiliation:
National Center for Microscopy and Imaging Research, Dept. of Neurosciences University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
T. Deerinck
Affiliation:
National Center for Microscopy and Imaging Research, Dept. of Neurosciences University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
M. Martone
Affiliation:
National Center for Microscopy and Imaging Research, Dept. of Neurosciences University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093. The San Diego Supercomputer Center University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
S. Adams
Affiliation:
Dept. of Pharmacology and the Howard Hughes Medical Institute, University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
A. Stelljes
Affiliation:
National Center for Microscopy and Imaging Research, Dept. of Neurosciences University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
K. Jordan
Affiliation:
Dept. of Anatomy and Cell Biology, University of Western Ontario, Ontario, CanadaN6A 5C1
D. W. Laird
Affiliation:
Dept. of Anatomy and Cell Biology, University of Western Ontario, Ontario, CanadaN6A 5C1
R. Tsien
Affiliation:
Dept. of Pharmacology and the Howard Hughes Medical Institute, University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093. Dept. of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
M. Ellisman
Affiliation:
National Center for Microscopy and Imaging Research, Dept. of Neurosciences University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093. The San Diego Supercomputer Center University of California, San Diego, 9500 Gilman Drive, La Jolla , CA, 92093.
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Abstract

Gap junction channels serve important functions for the homeostasis of organ systems. These membrane channels serve as low-resistance pathways for the diffusion of small molecular species such as ions, metabolites and second messengers between two neighboring cells (1). Recent intense investigations have been pursuing the effects that defects in gap junction proteins, the connexins, have in hereditary diseases. Mutations in the primary sequence of several connexins have been shown to be responsible for several hereditary human diseases including X-linked Charcot-Marie- Tooth demyelinating neuropathies, nonsyndromic sensorineural deafness, erythrokeratodermia and congenital cataractogenesis (c.f. (2, 3) for recent reviews). Many of the published mutations are being investigated thoroughly to determine at what stage and why the protein fails to make functional channels. Steps involved in connexin trafficking and assembly are: translation of the protein; transport from the endoplasmic reticulum to the Golgi apparatus; oligomerization of the subunits into a hexamer (called a connexon); transport of the connexon to non-junctional areas of the plasma membrane; correct docking with a partner connexon from an apposing cell to form a functional intercellular channel; and incorporation into aggregates (gap junction plaques).

Type
Electron Tomography: Recent Advances and Applications (Organized by M. Marko)
Information
Microscopy and Microanalysis , Volume 7 , Issue S2: Proceedings: Microscopy & Microanalysis 2001, Microscopy Society of America 59th Annual Meeting, Microbeam Analysis Society 35th Annual Meeting, Long Beach, California August 5-9, 2001 , August 2001 , pp. 80 - 81
Copyright
Copyright © Microscopy Society of America 2001

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References

references

1.Goodenough, D. A.et al., Ann. Rev. Biochem. 65: 475–502 (1996).CrossRefGoogle Scholar
2.Bennett, M. V. L. & Abrams, C. K., in Gap Junctions. Molecular basis of cell communication in health and disease. Peracchia, C., Ed. (Academic Press, San Diego, 2000), vol. 49, pp. 423–459.Google Scholar
3.Kelsell, D. P.et al. (2001) Trends Cell Biol. 11: 2–6.CrossRefGoogle Scholar
4.Laird, D. W., (1996) J. Bioenerg. Biomembr. 28: 311–318.CrossRefGoogle Scholar
5.Musil, L. S.et al. (1990) J.Cell Biol. III : 2077–2088.CrossRefGoogle Scholar
6.Jordan, K., et al., (1999) Mol. Biol. Cell 10: 2033–2050.CrossRefGoogle Scholar
7.Holm, I.et al. (1999)Eur. J. Cell Biology 78: 856–866.CrossRefGoogle Scholar
8.Hand, G. M.et al. (2000) Microsc. Res.Tech. 52: 331–343.3.0.CO;2-H>CrossRefGoogle Scholar
9.Griffin, A.G.et al. (1998) Science 281: 269–272.Funded by NSF grant MCB-9728338, NIH grants RR04050, DK54441, NS27177 and MRC grant MT12241.CrossRefGoogle Scholar