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Originally published In Press as doi:10.1074/jbc.M002608200 on June 2, 2000

J. Biol. Chem., Vol. 275, Issue 33, 25207-25215, August 18, 2000
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Regulation of Connexin Degradation as a Mechanism to Increase Gap Junction Assembly and Function*

Linda S. MusilDagger , Anh-Chi N. Le, Judy K. VanSlyke, and Lori M. Roberts

From the Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland, Oregon 97201

Connexins, the integral membrane protein constituents of gap junctions, are degraded at a rate (t1/2 = 1.5-5 h) much faster than most other cell surface proteins. Although the turnover of connexins has been shown to be sensitive to inhibitors of either the lysosome or of the proteasome, how connexins are targeted for degradation and whether this process can be regulated to affect intercellular communication is unknown. We show here that reducing connexin degradation with inhibitors of the proteasome (but not with lysosomal blockers) is associated with a striking increase in gap junction assembly and intercellular dye transfer in cells inefficient in both processes under basal conditions. The effect of proteasome inhibitors on wild-type connexin stability, assembly, and function was mimicked by treatment of assembly-inefficient cells with inhibitors of protein synthesis such as cycloheximide. Sensitivity of connexin degradation to cycloheximide, but not to proteasome inhibitors, was abolished when connexins were rendered structurally abnormal by perturbation of essential disulfide bonds or by mutation. Our findings provide the first evidence that intercellular communication can be up-regulated at the level of connexin turnover and that a short-lived protein may be required for conformationally mature connexins to become substrates of proteasomal degradation.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Vollum Institute for Advanced Biomedical Research L474, Oregon Health Sciences University, 3181 Southwest Sam Jackson Park Rd., Portland, OR 97201. Tel.: 503-494-1300; Fax: 503-494-8230; E-mail: Musill@ohsu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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