Cx43 has distinct mobility within plasma-membrane domains, indicative of progressive formation of gap-junction plaques
| Autor: | Jared M. Churko, Dale W. Laird, Qing Shao, Jamie Simek |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Cell signaling
Time Factors Recombinant Fusion Proteins Green Fluorescent Proteins Connexin Cell Surface Extension Cell Communication Biology Localization within membrane Animals Humans Microscopy Confocal Gap junction Fluorescence recovery after photobleaching Gap Junctions Biological Transport Cell Biology Protein Structure Tertiary Rats Membrane Connexin 43 cardiovascular system Cluster size Biophysics sense organs Cell Surface Extensions biological phenomena cell phenomena and immunity Fluorescence Recovery After Photobleaching HeLa Cells |
| Zdroj: | Journal of cell science. 122(Pt 4) |
| ISSN: | 0021-9533 |
| Popis: | Connexin 43 (Cx43) is a dynamic molecule, having a short half-life of only a few hours. In this study, we use fluorescent-protein-tagged Cx43 variants to examine Cx43 delivery to the cell surface, its residency status in various cell-surface membrane domains and its mobility characteristics. Rapid time-lapse imaging led to the identification of Cx43 being delivered to cell-surface domains that lacked a contacting cell, and also to its localization within membrane protrusions. Fluorescence recovery after photobleaching (FRAP) was used to investigate the mobility state of cell-surface-localized Cx43. Cx43 mobility within clustered cell-surface profiles of Cx43 could be categorized into those with generally a high degree of lateral mobility and those with generally a low degree of lateral mobility. Cx43 mobility was independent of cluster size, yet the C-terminal domain of Cx43 regulated the proportion of gap-junction-like clusters that acquired a low Cx43 mobility state. Collectively, these studies show that Cx43 establishes residency at all cell-surface membrane domains, and progressively acquires assembly states that probably reflect differences in either channel packing and/or its interactions with Cx43-binding proteins. |
| Databáze: | OpenAIRE |
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