The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants

The Arabidopsis CC1 protein maintains microtubule array stability and cellulose synthesis during salt stress. Here the authors show that CC1 engages microtubules via an intrinsically disordered N-terminus that suggests it controls microtubule dynamics in a similar way to the mammalian Tau protein.

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Autores principales: Christopher Kesten, Arndt Wallmann, René Schneider, Heather E. McFarlane, Anne Diehl, Ghazanfar Abbas Khan, Barth-Jan van Rossum, Edwin R. Lampugnani, Witold G. Szymanski, Nils Cremer, Peter Schmieder, Kristina L. Ford, Florian Seiter, Joshua L. Heazlewood, Clara Sanchez-Rodriguez, Hartmut Oschkinat, Staffan Persson
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/87145081be054b2c92c39b0951f10ce5
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spelling oai:doaj.org-article:87145081be054b2c92c39b0951f10ce52021-12-02T15:35:09ZThe companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants10.1038/s41467-019-08780-32041-1723https://doaj.org/article/87145081be054b2c92c39b0951f10ce52019-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08780-3https://doaj.org/toc/2041-1723The Arabidopsis CC1 protein maintains microtubule array stability and cellulose synthesis during salt stress. Here the authors show that CC1 engages microtubules via an intrinsically disordered N-terminus that suggests it controls microtubule dynamics in a similar way to the mammalian Tau protein.Christopher KestenArndt WallmannRené SchneiderHeather E. McFarlaneAnne DiehlGhazanfar Abbas KhanBarth-Jan van RossumEdwin R. LampugnaniWitold G. SzymanskiNils CremerPeter SchmiederKristina L. FordFlorian SeiterJoshua L. HeazlewoodClara Sanchez-RodriguezHartmut OschkinatStaffan PerssonNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Christopher Kesten
Arndt Wallmann
René Schneider
Heather E. McFarlane
Anne Diehl
Ghazanfar Abbas Khan
Barth-Jan van Rossum
Edwin R. Lampugnani
Witold G. Szymanski
Nils Cremer
Peter Schmieder
Kristina L. Ford
Florian Seiter
Joshua L. Heazlewood
Clara Sanchez-Rodriguez
Hartmut Oschkinat
Staffan Persson
The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
description The Arabidopsis CC1 protein maintains microtubule array stability and cellulose synthesis during salt stress. Here the authors show that CC1 engages microtubules via an intrinsically disordered N-terminus that suggests it controls microtubule dynamics in a similar way to the mammalian Tau protein.
format article
author Christopher Kesten
Arndt Wallmann
René Schneider
Heather E. McFarlane
Anne Diehl
Ghazanfar Abbas Khan
Barth-Jan van Rossum
Edwin R. Lampugnani
Witold G. Szymanski
Nils Cremer
Peter Schmieder
Kristina L. Ford
Florian Seiter
Joshua L. Heazlewood
Clara Sanchez-Rodriguez
Hartmut Oschkinat
Staffan Persson
author_facet Christopher Kesten
Arndt Wallmann
René Schneider
Heather E. McFarlane
Anne Diehl
Ghazanfar Abbas Khan
Barth-Jan van Rossum
Edwin R. Lampugnani
Witold G. Szymanski
Nils Cremer
Peter Schmieder
Kristina L. Ford
Florian Seiter
Joshua L. Heazlewood
Clara Sanchez-Rodriguez
Hartmut Oschkinat
Staffan Persson
author_sort Christopher Kesten
title The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
title_short The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
title_full The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
title_fullStr The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
title_full_unstemmed The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants
title_sort companion of cellulose synthase 1 confers salt tolerance through a tau-like mechanism in plants
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/87145081be054b2c92c39b0951f10ce5
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