Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Kyle JW 

PROVIDER: S-EPMC2752142 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Kyle John W JW   Minogue Peter J PJ   Thomas Bettina C BC   Domowicz Denise A Lopez DA   Berthoud Viviana M VM   Hanck Dorothy A DA   Beyer Eric C EC  

Journal of cell science 20080729 Pt 16


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 m  ...[more]

Similar Datasets

| S-EPMC5034775 | biostudies-literature
| S-EPMC3089535 | biostudies-literature
| S-EPMC3010190 | biostudies-literature
| S-EPMC3248906 | biostudies-literature
| S-EPMC3244566 | biostudies-literature
| S-EPMC3973107 | biostudies-literature
| S-EPMC3655668 | biostudies-literature
| S-EPMC1221976 | biostudies-other
| S-EPMC1479757 | biostudies-other
| S-EPMC3084674 | biostudies-literature