Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms10430
Title: Pin1At regulates PIN1 polar localization and root gravitropism
Authors: Xi, W 
Gong, X 
Yang, Q 
Yu, H 
Liou, Y.-C 
Keywords: auxin
peptidylprolyl isomerase Pin1
phosphoprotein phosphatase 2A
pin1At protein
unclassified drug
Arabidopsis protein
carrier protein
NIMA interacting peptidylprolyl isomerase
peptidylprolyl isomerase
phosphoprotein phosphatase 2
PIN1 protein, Arabidopsis
PIN1AT protein, Arabidopsis
PINOID protein, Arabidopsis
protein serine threonine kinase
antagonism
cells and cell components
enzyme activity
gene expression
gravity field
growth modeling
hormone
phenotype
protein
root system
Article
auxin transport
conformational transition
down regulation
gravitropism
nonhuman
phenotype
protein expression
protein localization
protein motif
protein phosphorylation
root gravitropism
Arabidopsis
enzymology
gene expression regulation
genetics
growth, development and aging
metabolism
plant root
protein transport
Arabidopsis
Arabidopsis Proteins
Gene Expression Regulation, Plant
Gravitropism
Membrane Transport Proteins
NIMA-Interacting Peptidylprolyl Isomerase
Peptidylprolyl Isomerase
Plant Roots
Protein Phosphatase 2
Protein Transport
Protein-Serine-Threonine Kinases
Issue Date: 2016
Publisher: Nature Publishing Group
Citation: Xi, W, Gong, X, Yang, Q, Yu, H, Liou, Y.-C (2016). Pin1At regulates PIN1 polar localization and root gravitropism. Nature Communications 7 : 10430. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms10430
Abstract: Root gravitropism allows plants to establish root systems and its regulation depends on polar auxin transport mediated by PIN-FORMED (PIN) auxin transporters. PINOID (PID) and PROTEIN PHOSPHATASE 2A (PP2A) act antagonistically on reversible phosphorylation of PINs. This regulates polar PIN distribution and auxin transport. Here we show that a peptidyl-prolyl cis/trans isomerase Pin1At regulates root gravitropism. Downregulation of Pin1At suppresses root agravitropic phenotypes of pp2aa and 35S:PID, while overexpression of Pin1At affects root gravitropic responses and enhances the pp2aa agravitropic phenotype. Pin1At also affects auxin transport and polar localization of PIN1 in stele cells, which is mediated by PID and PP2A. Furthermore, Pin1At catalyses the conformational change of the phosphorylated Ser/Thr-Pro motifs of PIN1. Thus, Pin1At mediates the conformational dynamics of PIN1 and affects PID- and PP2A-mediated regulation of PIN1 polar localization, which correlates with the regulation of root gravitropism.
Source Title: Nature Communications
URI: https://scholarbank.nus.edu.sg/handle/10635/175439
ISSN: 20411723
DOI: 10.1038/ncomms10430
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