Desmosome dualism – most of the junction is stable, but a plakophilin moiety is persistently dynamic
| Autor: | David Liebl, Graham D. Wright, Christoph Ballestrem, David R Garrod, Jaron Liu, Rogerio Alves de Almeida, Henri Huppert, Bian Yanes, E. Birgitte Lane, Judith B Fülle |
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| Rok vydání: | 2021 |
| Předmět: |
Desmoplakin
Cell Membrane Plakoglobin Desmosomes Cell Biology Desmocollins Biology Cadherins Desmoglein Cell biology medicine.anatomical_structure Desmoplakins Desmosome medicine biology.protein Humans gamma Catenin Desmosomal Cadherins Desmogleins Intermediate filament Plakophilins Research Article |
| Zdroj: | J Cell Sci |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | Desmosomes, strong cell–cell junctions of epithelia and cardiac muscle, link intermediate filaments to cell membranes and mechanically integrate cells across tissues, dissipating mechanical stress. They comprise five major protein classes – desmocollins and desmogleins (the desmosomal cadherins), plakoglobin, plakophilins and desmoplakin – whose individual contribution to the structure and turnover of desmosomes is poorly understood. Using live-cell imaging together with fluorescence recovery after photobleaching (FRAP) and fluorescence loss and localisation after photobleaching (FLAP), we show that desmosomes consist of two contrasting protein moieties or modules: a very stable moiety of desmosomal cadherins, desmoplakin and plakoglobin, and a highly mobile plakophilin (Pkp2a). As desmosomes mature from Ca2+ dependence to Ca2+-independent hyper-adhesion, their stability increases, but Pkp2a remains highly mobile. We show that desmosome downregulation during growth-factor-induced cell scattering proceeds by internalisation of whole desmosomes, which still retain a stable moiety and highly mobile Pkp2a. This molecular mobility of Pkp2a suggests a transient and probably regulatory role for Pkp2a in desmosomes. This article has an associated First Person interview with the first author of the paper. |
| Databáze: | OpenAIRE |
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