Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic.Citation formats

  • External authors:
  • Judith B. Fülle
  • Henri Huppert
  • David Liebl
  • Jaron Liu
  • Rogerio Alves de Almeida
  • Bian Yanes
  • Graham D. Wright
  • E Birgitte Lane
  • David Garrod

Standard

Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic. / Fülle, Judith B.; Huppert, Henri; Liebl, David; Liu, Jaron; de Almeida, Rogerio Alves; Yanes, Bian; Wright, Graham D.; Lane, E Birgitte; Garrod, David; Ballestrem, Christoph.

In: Journal of Cell Science, 05.10.2021.

Research output: Contribution to journalArticlepeer-review

Harvard

Fülle, JB, Huppert, H, Liebl, D, Liu, J, de Almeida, RA, Yanes, B, Wright, GD, Lane, EB, Garrod, D & Ballestrem, C 2021, 'Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic.', Journal of Cell Science.

APA

Fülle, J. B., Huppert, H., Liebl, D., Liu, J., de Almeida, R. A., Yanes, B., Wright, G. D., Lane, E. B., Garrod, D., & Ballestrem, C. (Accepted/In press). Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic. Journal of Cell Science.

Vancouver

Fülle JB, Huppert H, Liebl D, Liu J, de Almeida RA, Yanes B et al. Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic. Journal of Cell Science. 2021 Oct 5.

Author

Fülle, Judith B. ; Huppert, Henri ; Liebl, David ; Liu, Jaron ; de Almeida, Rogerio Alves ; Yanes, Bian ; Wright, Graham D. ; Lane, E Birgitte ; Garrod, David ; Ballestrem, Christoph. / Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic. In: Journal of Cell Science. 2021.

Bibtex

@article{e14b71140850413f8bf6e00fd794e069,
title = "Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic.",
abstract = "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 FRAP and 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 calcium-dependence to calcium-independent hyper-adhesion, their stability increases, but Pkp2a remains highly mobile. We show that desmosome down-regulation 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.",
author = "F{\"u}lle, {Judith B.} and Henri Huppert and David Liebl and Jaron Liu and {de Almeida}, {Rogerio Alves} and Bian Yanes and Wright, {Graham D.} and Lane, {E Birgitte} and David Garrod and Christoph Ballestrem",
year = "2021",
month = oct,
day = "5",
language = "English",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",

}

RIS

TY - JOUR

T1 - Desmosome dualism: most of the junction is stable but a plakophilin moiety is persistently dynamic.

AU - Fülle, Judith B.

AU - Huppert, Henri

AU - Liebl, David

AU - Liu, Jaron

AU - de Almeida, Rogerio Alves

AU - Yanes, Bian

AU - Wright, Graham D.

AU - Lane, E Birgitte

AU - Garrod, David

AU - Ballestrem, Christoph

PY - 2021/10/5

Y1 - 2021/10/5

N2 - 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 FRAP and 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 calcium-dependence to calcium-independent hyper-adhesion, their stability increases, but Pkp2a remains highly mobile. We show that desmosome down-regulation 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.

AB - 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 FRAP and 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 calcium-dependence to calcium-independent hyper-adhesion, their stability increases, but Pkp2a remains highly mobile. We show that desmosome down-regulation 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.

M3 - Article

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

ER -