Advanced search
1 file | 1.29 MB Add to list

A novel protein family mediates Casparian strip formation in the endodermis

(2011) NATURE. 473(7347). p.380-U564
Author
Organization
Abstract
Polarized epithelia are fundamental to multicellular life. In animal epithelia, conserved junctional complexes establish membrane diffusion barriers, cellular adherence and sealing of the extracellular space(1). Plant cellular barriers are of independent evolutionary origin. The root endodermis strongly resembles a polarized epithelium and functions in nutrient uptake and stress resistance(2). Its defining features are the Casparian strips, belts of specialized cell wall material that generate an extracellular diffusion barrier(2). The mechanisms localizing Casparian strips are unknown. Here we identify and characterize a family of transmembrane proteins of previously unknown function. These 'CASPs' (Casparian strip membrane domain proteins) specifically mark a membrane domain that predicts the formation of Casparian strips. CASP1 displays numerous features required for a constituent of a plant junctional complex: it forms complexes with other CASPs; it becomes immobile upon localization; and it sediments like a large polymer. CASP double mutants display disorganized Casparian strips, demonstrating a role for CASPs in structuring and localizing this cell wall modification. To our knowledge, CASPs are the first molecular factors that are shown to establish a plasma membrane and extracellular diffusion barrier in plants, and represent a novel way of epithelial barrier formation in eukaryotes.
Keywords
MOVEMENT, POLARITY, TRANSPORT, PLANT, ARABIDOPSIS ROOT, ASYMMETRIC CELL-DIVISION

Downloads

  • (...).pdf
    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 1.29 MB

Citation

Please use this url to cite or link to this publication:

MLA
Roppolo, Daniele, Bert De Rybel, Valérie Dénervaud Tendon, et al. “A Novel Protein Family Mediates Casparian Strip Formation in the Endodermis.” NATURE 473.7347 (2011): 380–U564. Print.
APA
Roppolo, D., De Rybel, B., Tendon, V. D., Pfister, A., Alassimone, J., Vermeer, J. E., Yamazaki, M., et al. (2011). A novel protein family mediates Casparian strip formation in the endodermis. NATURE, 473(7347), 380–U564.
Chicago author-date
Roppolo, Daniele, Bert De Rybel, Valérie Dénervaud Tendon, Alexandre Pfister, Julien Alassimone, Joop EM Vermeer, Misako Yamazaki, York-Dieter Stierhof, Tom Beeckman, and Niko Geldner. 2011. “A Novel Protein Family Mediates Casparian Strip Formation in the Endodermis.” Nature 473 (7347): 380–U564.
Chicago author-date (all authors)
Roppolo, Daniele, Bert De Rybel, Valérie Dénervaud Tendon, Alexandre Pfister, Julien Alassimone, Joop EM Vermeer, Misako Yamazaki, York-Dieter Stierhof, Tom Beeckman, and Niko Geldner. 2011. “A Novel Protein Family Mediates Casparian Strip Formation in the Endodermis.” Nature 473 (7347): 380–U564.
Vancouver
1.
Roppolo D, De Rybel B, Tendon VD, Pfister A, Alassimone J, Vermeer JE, et al. A novel protein family mediates Casparian strip formation in the endodermis. NATURE. 2011;473(7347):380–U564.
IEEE
[1]
D. Roppolo et al., “A novel protein family mediates Casparian strip formation in the endodermis,” NATURE, vol. 473, no. 7347, pp. 380-U564, 2011.
@article{1266393,
  abstract     = {Polarized epithelia are fundamental to multicellular life. In animal epithelia, conserved junctional complexes establish membrane diffusion barriers, cellular adherence and sealing of the extracellular space(1). Plant cellular barriers are of independent evolutionary origin. The root endodermis strongly resembles a polarized epithelium and functions in nutrient uptake and stress resistance(2). Its defining features are the Casparian strips, belts of specialized cell wall material that generate an extracellular diffusion barrier(2). The mechanisms localizing Casparian strips are unknown. Here we identify and characterize a family of transmembrane proteins of previously unknown function. These 'CASPs' (Casparian strip membrane domain proteins) specifically mark a membrane domain that predicts the formation of Casparian strips. CASP1 displays numerous features required for a constituent of a plant junctional complex: it forms complexes with other CASPs; it becomes immobile upon localization; and it sediments like a large polymer. CASP double mutants display disorganized Casparian strips, demonstrating a role for CASPs in structuring and localizing this cell wall modification. To our knowledge, CASPs are the first molecular factors that are shown to establish a plasma membrane and extracellular diffusion barrier in plants, and represent a novel way of epithelial barrier formation in eukaryotes.},
  author       = {Roppolo, Daniele and De Rybel, Bert and Tendon, Valérie Dénervaud  and Pfister, Alexandre and Alassimone, Julien and Vermeer, Joop EM and Yamazaki, Misako and Stierhof, York-Dieter and Beeckman, Tom and Geldner, Niko},
  issn         = {0028-0836},
  journal      = {NATURE},
  keywords     = {MOVEMENT,POLARITY,TRANSPORT,PLANT,ARABIDOPSIS ROOT,ASYMMETRIC CELL-DIVISION},
  language     = {eng},
  number       = {7347},
  pages        = {380--U564},
  title        = {A novel protein family mediates Casparian strip formation in the endodermis},
  url          = {http://dx.doi.org/10.1038/nature10070},
  volume       = {473},
  year         = {2011},
}

Altmetric
View in Altmetric
Web of Science
Times cited: