Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions
Cell-cell adhesion mediated by catenin-cadherin complexes plays a critical role in translating the mechanical forces into physiological responses. Here the authors define a mechanism of force-dependent cadherin-actin linkage dynamically regulated through the actin-binding domain of α-catenin.
Guardado en:
| Autores principales: | , , , , , , , , , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2018
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/811fe916ab7f4aa8a28b241ddb5f61db |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:doaj.org-article:811fe916ab7f4aa8a28b241ddb5f61db |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:811fe916ab7f4aa8a28b241ddb5f61db2021-12-02T14:40:31ZForce-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions10.1038/s41467-018-07481-72041-1723https://doaj.org/article/811fe916ab7f4aa8a28b241ddb5f61db2018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07481-7https://doaj.org/toc/2041-1723Cell-cell adhesion mediated by catenin-cadherin complexes plays a critical role in translating the mechanical forces into physiological responses. Here the authors define a mechanism of force-dependent cadherin-actin linkage dynamically regulated through the actin-binding domain of α-catenin.Noboru IshiyamaRitu SarpalMegan N. WoodSamantha K. BarrickTadateru NishikawaHanako HayashiAnna B. KobbAnnette S. FlozakAlex YemelyanovRodrigo Fernandez-GonzalezShigenobu YonemuraDeborah E. LeckbandCara J. GottardiUlrich TepassMitsuhiko IkuraNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-17 (2018) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Noboru Ishiyama Ritu Sarpal Megan N. Wood Samantha K. Barrick Tadateru Nishikawa Hanako Hayashi Anna B. Kobb Annette S. Flozak Alex Yemelyanov Rodrigo Fernandez-Gonzalez Shigenobu Yonemura Deborah E. Leckband Cara J. Gottardi Ulrich Tepass Mitsuhiko Ikura Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions |
| description |
Cell-cell adhesion mediated by catenin-cadherin complexes plays a critical role in translating the mechanical forces into physiological responses. Here the authors define a mechanism of force-dependent cadherin-actin linkage dynamically regulated through the actin-binding domain of α-catenin. |
| format |
article |
| author |
Noboru Ishiyama Ritu Sarpal Megan N. Wood Samantha K. Barrick Tadateru Nishikawa Hanako Hayashi Anna B. Kobb Annette S. Flozak Alex Yemelyanov Rodrigo Fernandez-Gonzalez Shigenobu Yonemura Deborah E. Leckband Cara J. Gottardi Ulrich Tepass Mitsuhiko Ikura |
| author_facet |
Noboru Ishiyama Ritu Sarpal Megan N. Wood Samantha K. Barrick Tadateru Nishikawa Hanako Hayashi Anna B. Kobb Annette S. Flozak Alex Yemelyanov Rodrigo Fernandez-Gonzalez Shigenobu Yonemura Deborah E. Leckband Cara J. Gottardi Ulrich Tepass Mitsuhiko Ikura |
| author_sort |
Noboru Ishiyama |
| title |
Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions |
| title_short |
Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions |
| title_full |
Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions |
| title_fullStr |
Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions |
| title_full_unstemmed |
Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions |
| title_sort |
force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions |
| publisher |
Nature Portfolio |
| publishDate |
2018 |
| url |
https://doaj.org/article/811fe916ab7f4aa8a28b241ddb5f61db |
| work_keys_str_mv |
AT noboruishiyama forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT ritusarpal forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT megannwood forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT samanthakbarrick forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT tadaterunishikawa forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT hanakohayashi forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT annabkobb forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT annettesflozak forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT alexyemelyanov forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT rodrigofernandezgonzalez forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT shigenobuyonemura forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT deboraheleckband forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT carajgottardi forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT ulrichtepass forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions AT mitsuhikoikura forcedependentallosteryoftheacateninactinbindingdomaincontrolsadherensjunctiondynamicsandfunctions |
| _version_ |
1718390248829878272 |