Ghent University Academic Bibliography

Advanced

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

Hongjiang Li, Deshu Lin, Pankaj Dhonukshe UGent, Shingo Nagawa, Dandan Chen, Jiri Friml UGent, Ben Scheres, Hongwei Guo and Zhenbiao Yang (2011) CELL RESEARCH. 21(6). p.970-978
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
Arabidopsis, pavement cells, protein kinase, PLANTS, GROWTH, MOTIFS, EFFLUX, POINTS, MORPHOGENESIS, PROTEIN-KINASE, POLARITY, protein phosphatase, PIN1 polarity, AUXIN TRANSPORT
journal title
CELL RESEARCH
Cell Res.
volume
21
issue
6
pages
970 - 978
Web of Science type
Article
Web of Science id
000291201600012
JCR category
CELL BIOLOGY
JCR impact factor
8.19 (2011)
JCR rank
23/178 (2011)
JCR quartile
1 (2011)
ISSN
1001-0602
DOI
10.1038/cr.2011.49
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1854252
handle
http://hdl.handle.net/1854/LU-1854252
date created
2011-07-06 17:55:01
date last changed
2013-09-17 11:17:49
@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},
  keyword      = {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://dx.doi.org/10.1038/cr.2011.49},
  volume       = {21},
  year         = {2011},
}

Chicago
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.
APA
Li, Hongjiang, Lin, D., Dhonukshe, P., Nagawa, S., Chen, D., Friml, J., Scheres, B., et al. (2011). Phosphorylation switch modulates the interdigitated pattern of PIN1 localization and cell expansion in Arabidopsis leaf epidermis. CELL RESEARCH, 21(6), 970–978.
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.
MLA
Li, Hongjiang, Deshu Lin, Pankaj Dhonukshe, et al. “Phosphorylation Switch Modulates the Interdigitated Pattern of PIN1 Localization and Cell Expansion in Arabidopsis Leaf Epidermis.” CELL RESEARCH 21.6 (2011): 970–978. Print.