PUBLICATION
Cx23, a connexin with only four extracellular-loop cysteines, forms functional gap junction channels and hemichannels
- Authors
- Iovine, M.K., Gumpert, A.M., Falk, M.M., and Mendelson, T.C.
- ID
- ZDB-PUB-071219-2
- Date
- 2008
- Source
- FEBS letters 582(2): 165-170 (Journal)
- Registered Authors
- Iovine, M. Kathryn
- Keywords
- Gap junction, Connexin, Zebrafish, Pannexin, Cx23
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- Connexins/chemistry
- Connexins/physiology*
- Cysteine/chemistry*
- DNA Primers
- Gap Junctions/chemistry
- Gap Junctions/physiology*
- HeLa Cells
- Humans
- In Situ Hybridization
- Lens, Crystalline/metabolism
- Molecular Sequence Data
- Sequence Homology, Amino Acid
- Zebrafish
- PubMed
- 18068130 Full text @ FEBS Lett.
Citation
Iovine, M.K., Gumpert, A.M., Falk, M.M., and Mendelson, T.C. (2008) Cx23, a connexin with only four extracellular-loop cysteines, forms functional gap junction channels and hemichannels. FEBS letters. 582(2):165-170.
Abstract
Gap junction channels may be comprised of either connexin or pannexin proteins (innexins and pannexins). Membrane topologies of both families are similar, but sequence similarity is lacking. Recently, connexin-like sequences have been identified in mammalian and zebrafish genomes that have only four conserved cysteines in the extracellular domains (Cx23), a feature of the pannexins. Phylogenetic analyses of the non-canonical "C4" connexins reveal that these sequences are indeed connexins. Functional assays reveal that the Cx23 gap junctions are capable of sharing neurobiotin, and further, that Cx23 connexins form hemichannels in vitro.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping