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A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation and auxin efflux in Arabidopsis

Mingqiu Dai, Chen Zhang, Urszula Kania UGent, Fang Chen, Qin Xue, Tyra Mccray, Gang Li, Genji Qin, Michelle Wakeley and William Terzaghi, et al. (2012) PLANT CELL. 24(6). p.2497-2514
abstract
The directional transport of the phytohormone auxin depends on the phosphorylation status and polar localization of PIN-FORMED (PIN) auxin efflux proteins. While PINIOD (PID) kinase is directly involved in the phosphorylation of PIN proteins, the phosphatase holoenzyme complexes that dephosphorylate PIN proteins remain elusive. Here, we demonstrate that mutations simultaneously disrupting the function of Arabidopsis thaliana FyPP1 (for Phytochrome-associated serine/threonine protein phosphatase1) and FyPP3, two homologous genes encoding the catalytic subunits of protein phosphatase6 (PP6), cause elevated accumulation of phosphorylated PIN proteins, correlating with a basal-to-apical shift in subcellular PIN localization. The changes in PIN polarity result in increased root basipetal auxin transport and severe defects, including shorter roots, fewer lateral roots, defective columella cells, root meristem collapse, abnormal cotyledons (small, cup-shaped, or fused cotyledons), and altered leaf venation. Our molecular, biochemical, and genetic data support the notion that FyPP1/3, SAL (for SAPS DOMAIN-LIKE), and PP2AA proteins (RCN1 [for ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID1] or PP2AA1, PP2AA2, and PP2AA3) physically interact to form a novel PP6-type heterotrimeric holoenzyme complex. We also show that FyPP1/3, SAL, and PP2AA interact with a subset of PIN proteins and that for SAL the strength of the interaction depends on the PIN phosphorylation status. Thus, an Arabidopsis PP6-type phosphatase holoenzyme acts antagonistically with PID to direct auxin transport polarity and plant development by directly regulating PIN phosphorylation.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
PROTEIN-PROTEIN INTERACTIONS, TRANSCRIPTION FACTOR, GRADIENTS ESTABLISH, P-GLYCOPROTEIN, CELL POLARITY, TRANSPORT, KINASE, LOCALIZATION, PLANTS, SUBUNIT
journal title
PLANT CELL
Plant Cell
volume
24
issue
6
pages
2497 - 2514
Web of Science type
Article
Web of Science id
000306919300021
JCR category
PLANT SCIENCES
JCR impact factor
9.251 (2012)
JCR rank
4/193 (2012)
JCR quartile
1 (2012)
ISSN
1040-4651
DOI
10.1105/tpc.112.098905
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2985822
handle
http://hdl.handle.net/1854/LU-2985822
date created
2012-09-12 15:08:49
date last changed
2012-12-17 16:39:19
@article{2985822,
  abstract     = {The directional transport of the phytohormone auxin depends on the phosphorylation status and polar localization of PIN-FORMED (PIN) auxin efflux proteins. While PINIOD (PID) kinase is directly involved in the phosphorylation of PIN proteins, the phosphatase holoenzyme complexes that dephosphorylate PIN proteins remain elusive. Here, we demonstrate that mutations simultaneously disrupting the function of Arabidopsis thaliana FyPP1 (for Phytochrome-associated serine/threonine protein phosphatase1) and FyPP3, two homologous genes encoding the catalytic subunits of protein phosphatase6 (PP6), cause elevated accumulation of phosphorylated PIN proteins, correlating with a basal-to-apical shift in subcellular PIN localization. The changes in PIN polarity result in increased root basipetal auxin transport and severe defects, including shorter roots, fewer lateral roots, defective columella cells, root meristem collapse, abnormal cotyledons (small, cup-shaped, or fused cotyledons), and altered leaf venation. Our molecular, biochemical, and genetic data support the notion that FyPP1/3, SAL (for SAPS DOMAIN-LIKE), and PP2AA proteins (RCN1 [for ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID1] or PP2AA1, PP2AA2, and PP2AA3) physically interact to form a novel PP6-type heterotrimeric holoenzyme complex. We also show that FyPP1/3, SAL, and PP2AA interact with a subset of PIN proteins and that for SAL the strength of the interaction depends on the PIN phosphorylation status. Thus, an Arabidopsis PP6-type phosphatase holoenzyme acts antagonistically with PID to direct auxin transport polarity and plant development by directly regulating PIN phosphorylation.},
  author       = {Dai, Mingqiu and Zhang, Chen and Kania, Urszula and Chen, Fang and Xue, Qin and Mccray, Tyra and Li, Gang and Qin, Genji and Wakeley, Michelle and Terzaghi, William and Wan, Jianmin and Zhao, Yunde and Xu, Jian and Friml, Jiri and Deng, Xing Wang and Wang, Haiyang},
  issn         = {1040-4651},
  journal      = {PLANT CELL},
  keyword      = {PROTEIN-PROTEIN INTERACTIONS,TRANSCRIPTION FACTOR,GRADIENTS ESTABLISH,P-GLYCOPROTEIN,CELL POLARITY,TRANSPORT,KINASE,LOCALIZATION,PLANTS,SUBUNIT},
  language     = {eng},
  number       = {6},
  pages        = {2497--2514},
  title        = {A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation and auxin efflux in Arabidopsis},
  url          = {http://dx.doi.org/10.1105/tpc.112.098905},
  volume       = {24},
  year         = {2012},
}

Chicago
Dai, Mingqiu, Chen Zhang, Urszula Kania, Fang Chen, Qin Xue, Tyra Mccray, Gang Li, et al. 2012. “A PP6-type Phosphatase Holoenzyme Directly Regulates PIN Phosphorylation and Auxin Efflux in Arabidopsis.” Plant Cell 24 (6): 2497–2514.
APA
Dai, M., Zhang, C., Kania, U., Chen, F., Xue, Q., Mccray, T., Li, G., et al. (2012). A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation and auxin efflux in Arabidopsis. PLANT CELL, 24(6), 2497–2514.
Vancouver
1.
Dai M, Zhang C, Kania U, Chen F, Xue Q, Mccray T, et al. A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation and auxin efflux in Arabidopsis. PLANT CELL. 2012;24(6):2497–514.
MLA
Dai, Mingqiu, Chen Zhang, Urszula Kania, et al. “A PP6-type Phosphatase Holoenzyme Directly Regulates PIN Phosphorylation and Auxin Efflux in Arabidopsis.” PLANT CELL 24.6 (2012): 2497–2514. Print.