scholarly journals Regulation of a plant aquaporin by a Casparian strip membrane domain protein‐like

2019 ◽  
Vol 42 (6) ◽  
pp. 1788-1801 ◽  
Author(s):  
Chloé Champeyroux ◽  
Jorge Bellati ◽  
Marie Barberon ◽  
Valérie Rofidal ◽  
Christophe Maurel ◽  
...  
2019 ◽  
Vol 106 (Spl) ◽  
Author(s):  
Mandlik Rushil ◽  
Varanavasiappan S ◽  
Kumar K K ◽  
Kokiladevi E ◽  
Sudhakar D ◽  
...  

2014 ◽  
Vol 165 (4) ◽  
pp. 1709-1722 ◽  
Author(s):  
Daniele Roppolo ◽  
Brigitte Boeckmann ◽  
Alexandre Pfister ◽  
Emmanuel Boutet ◽  
Maria C. Rubio ◽  
...  

BMC Genomics ◽  
2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Xiaoyang Wang ◽  
Yuanming Zhang ◽  
Liyuan Wang ◽  
Zhaoe Pan ◽  
Shoupu He ◽  
...  

2020 ◽  
Vol 117 (27) ◽  
pp. 15400-15402 ◽  
Author(s):  
Yan Zhuang ◽  
Daqing Zuo ◽  
Yihan Tao ◽  
Huaqing Cai ◽  
Lei Li

The Casparian strip (CS) is a tight junction-like structure formed by lignin impregnation on the walls of endodermal cells in plant roots. The CS membrane domain (CSDM), demarked by the CASP proteins, is important for orienting lignification enzymes. Here, we report that an endodermis-expressed multicopper oxidase, LACCASE3 (LAC3) inArabidopsis, locates to the interface between lignin domains and the cell wall during early CS development prior to CASP1 localizing to CSDMand eventually flanks the mature CS. Pharmacological perturbation of LAC3 causes dispersed localization of CASP1 and compensatory ectopic lignification. These results support the existence of a LAC3-based CS wall domain which coordinates with CSDMto provide bidirectional positional information that guides precise CS lignification.


2009 ◽  
Vol 40 (01) ◽  
Author(s):  
J Schessl ◽  
Y Zou ◽  
MJ McGrath ◽  
BS Cowling ◽  
B Maiti ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document