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First published online 29 July 2008
doi: 10.1242/jcs.032482

Journal of Cell Science 121, 2744-2750 (2008)
Published by The Company of Biologists 2008
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Research Article

An intact connexin N-terminus is required for function but not gap junction formation

John W. Kyle1, Peter J. Minogue2, Bettina C. Thomas2, Denise A. Lopez Domowicz2, Viviana M. Berthoud2, Dorothy A. Hanck1 and Eric C. Beyer2,*

1 Department of Medicine, Section of Cardiology, University of Chicago, Chicago, IL 60637, USA
2 Department of Pediatrics, Section of Hematology/Oncology, University of Chicago, Chicago, IL 60637, USA

* Author for correspondence (e-mail: ebeyer{at}peds.bsd.uchicago.edu)

Accepted 9 June 2008

The cytoplasmic N-termini of connexins have been implicated in protein trafficking, oligomerization and channel gating. To elucidate the role of the N-terminus in connexin37 (CX37), we studied mutant constructs containing partial deletions of its 23 N-terminal amino acids and a construct with a complete N-terminus in which residues 2-8 were replaced with alanines. All mutants containing nine or more N-terminal amino acids form gap junction plaques in transiently transfected HeLa cells, whereas most of the longer deletions do not. Although wild-type CX37 allowed intercellular transfer of microinjected neurobiotin in HeLa cells and formed conducting hemichannels in Xenopus oocytes, none of the mutant constructs tested show evidence of channel function. However, in coexpression experiments, N-terminal mutants that formed gap junction plaques potently inhibit hemichannel conductance of wild-type CX37 suggesting their co-oligomerization. We conclude that as much as half the length of the connexin N-terminus can be deleted without affecting formation of gap junction plaques, but an intact N-terminus is required for hemichannel gating and intercellular communication.

Key words: Connexin37, Gap junction, Intercellular communication


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J. W. Kyle, V. M. Berthoud, J. Kurutz, P. J. Minogue, M. Greenspan, D. A. Hanck, and E. C. Beyer
The N Terminus of Connexin37 Contains an {alpha}-Helix That Is Required for Channel Function
J. Biol. Chem., July 24, 2009; 284(30): 20418 - 20427.
[Abstract] [Full Text] [PDF]


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