Advanced search
1 file | 1.08 MB Add to list

Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis

(2011) CELL RESEARCH. 21(6). p.970-978
Author
Organization
Abstract
Within a multicellular tissue cells may coordinately form a singular or multiple polar axes, but it is unclear whether a common mechanism governs different types of polar axis formation. The phosphorylation status of PIN proteins, which is directly affected by the PINOID (PID) protein kinase and the PP2A protein phosphatase, is known to regulate the apical-basal polarity of PIN localization in bipolar cells of roots and shoot apices. Here, we provide evidence that the phosphorylation status-mediated PIN polarity switch is widely used to modulate cellular processes in Arabidopsis including multipolar pavement cells (PC) with interdigitated lobes and indentations. The degree of PC interdigitation was greatly reduced either when the FYPP1 gene, which encodes a PP2A called phytochrome-associated serine/threonine protein phosphatase, was knocked out or when the PID gene was overexpressed (35S::PID). These genetic modifications caused PIN1 localization to switch from lobe to indentation regions. The PP2A and PID mediated switching of PIN1 localization is strikingly similar to their regulation of the apical-basal polarity switch of PIN proteins in other cells. Our findings suggest a common mechanism for the regulation of PIN1 polarity formation, a fundamental cellular process that is crucial for pattern formation both at the tissue/organ and cellular levels.
Keywords
Arabidopsis, pavement cells, protein kinase, PLANTS, GROWTH, MOTIFS, EFFLUX, POINTS, MORPHOGENESIS, PROTEIN-KINASE, POLARITY, protein phosphatase, PIN1 polarity, AUXIN TRANSPORT

Downloads

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

Citation

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

MLA
Li, Hongjiang, et al. “Phosphorylation Switch Modulates the Interdigitated Pattern of PIN1 Localization and Cell Expansion in Arabidopsis Leaf Epidermis.” CELL RESEARCH, vol. 21, no. 6, 2011, pp. 970–78, doi:10.1038/cr.2011.49.
APA
Li, H., Lin, D., Dhonukshe, P., Nagawa, S., Chen, D., Friml, J., … Yang, Z. (2011). Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis. CELL RESEARCH, 21(6), 970–978. https://doi.org/10.1038/cr.2011.49
Chicago author-date
Li, Hongjiang, Deshu Lin, Pankaj Dhonukshe, Shingo Nagawa, Dandan Chen, Jiri Friml, Ben Scheres, Hongwei Guo, and Zhenbiao Yang. 2011. “Phosphorylation Switch Modulates the Interdigitated Pattern of PIN1 Localization and Cell Expansion in Arabidopsis Leaf Epidermis.” CELL RESEARCH 21 (6): 970–78. https://doi.org/10.1038/cr.2011.49.
Chicago author-date (all authors)
Li, Hongjiang, Deshu Lin, Pankaj Dhonukshe, Shingo Nagawa, Dandan Chen, Jiri Friml, Ben Scheres, Hongwei Guo, and Zhenbiao Yang. 2011. “Phosphorylation Switch Modulates the Interdigitated Pattern of PIN1 Localization and Cell Expansion in Arabidopsis Leaf Epidermis.” CELL RESEARCH 21 (6): 970–978. doi:10.1038/cr.2011.49.
Vancouver
1.
Li H, Lin D, Dhonukshe P, Nagawa S, Chen D, Friml J, et al. Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis. CELL RESEARCH. 2011;21(6):970–8.
IEEE
[1]
H. Li et al., “Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis,” CELL RESEARCH, vol. 21, no. 6, pp. 970–978, 2011.
@article{1854252,
  abstract     = {{Within a multicellular tissue cells may coordinately form a singular or multiple polar axes, but it is unclear whether a common mechanism governs different types of polar axis formation. The phosphorylation status of PIN proteins, which is directly affected by the PINOID (PID) protein kinase and the PP2A protein phosphatase, is known to regulate the apical-basal polarity of PIN localization in bipolar cells of roots and shoot apices. Here, we provide evidence that the phosphorylation status-mediated PIN polarity switch is widely used to modulate cellular processes in Arabidopsis including multipolar pavement cells (PC) with interdigitated lobes and indentations. The degree of PC interdigitation was greatly reduced either when the FYPP1 gene, which encodes a PP2A called phytochrome-associated serine/threonine protein phosphatase, was knocked out or when the PID gene was overexpressed (35S::PID). These genetic modifications caused PIN1 localization to switch from lobe to indentation regions. The PP2A and PID mediated switching of PIN1 localization is strikingly similar to their regulation of the apical-basal polarity switch of PIN proteins in other cells. Our findings suggest a common mechanism for the regulation of PIN1 polarity formation, a fundamental cellular process that is crucial for pattern formation both at the tissue/organ and cellular levels.}},
  author       = {{Li, Hongjiang and Lin, Deshu and Dhonukshe, Pankaj and Nagawa, Shingo and Chen, Dandan and Friml, Jiri and Scheres, Ben and Guo, Hongwei and Yang, Zhenbiao}},
  issn         = {{1001-0602}},
  journal      = {{CELL RESEARCH}},
  keywords     = {{Arabidopsis,pavement cells,protein kinase,PLANTS,GROWTH,MOTIFS,EFFLUX,POINTS,MORPHOGENESIS,PROTEIN-KINASE,POLARITY,protein phosphatase,PIN1 polarity,AUXIN TRANSPORT}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{970--978}},
  title        = {{Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis}},
  url          = {{http://doi.org/10.1038/cr.2011.49}},
  volume       = {{21}},
  year         = {{2011}},
}

Altmetric
View in Altmetric
Web of Science
Times cited: