PbSnRK1-Mediated Phosphorylation of PbTCP13 Regulates Glucose-Responsive Lignin Biosynthesis via PbMYB11 During Pear Stone Cell Formation.
4 affiliations
- 1Sanya Institute, State Key Laboratory of Crop Genetics and Germplasm Enhancement, College of Horticulture, Nanjing Agricultural University, Nanjing, China.
- 2State Key Laboratory of Ecological Safety and Sustainable Development in Arid Lands, Xinjiang Institute of Ecology and Geography, Chinese Academy of Sciences, Urumqi, China.
- 3Laboratory of Horticultural Science, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
- 4Elm Consulting, Genetic Research, St-Lazare, Quebec, Canada.
Abstract
Stone cell lignification is a key determinant of pear fruit texture and commercial quality, and this process has been reported to be tightly coupled to cellular glucose availability. However, how glucose dose-dependently targets transcription factor phosphorylation during lignin biosynthesis remains largely unknown. Using yeast two-hybrid library screening and phosphorylation assays, we found that PbSnRK1, a glucose-responsive kinase, interacts with and directly phosphorylates PbTCP13, thereby participating in the regulation of stone cell lignification. PbSnRK1 serves as an energy-status sensor linking glucose signalling to biphasic regulation of lignin metabolism in pear. Under low-glucose conditions, activated PbSnRK1 phosphorylates the transcription factor PbTCP13 at Ser265, targeting it for 26S proteasome-mediated degradation and thereby derepressing PbMYB11-PbCCR1 cascade associated with lignin biosynthesis. Under high-glucose conditions, suppressed PbSnRK1 kinase activity results in PbTCP13 protein accumulation, which restricts excessive lignification by both repressing PbCCR1 transcription and physically interacting with PbMYB11 to inhibit its transactivation capacity. This PbSnRK1-PbTCP13-PbMYB11 cascade, balanced by glucose concentration, acts as a molecular switch that activates stone cell formation and lignification at low-glucose levels during early fruit development, while restricting excessive lignification at high-glucose levels during later stages, providing new mechanistic insights into energy-coupled secondary wall metabolism in fleshy fruits.
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BibTeX
@article{he2026pbsnrk1mediated,
title = {{PbSnRK1-Mediated Phosphorylation of PbTCP13 Regulates Glucose-Responsive Lignin Biosynthesis via PbMYB11 During Pear Stone Cell Formation.}},
author = {Jianan He and Xuxu Wang and Abdul Basit and Wen Li and Jiahui Chao and Wenyu Zhao and Mingxu Niu and Xin Yan and Yuanhui Yu and Kaijie Qi and Zhihua Xie and Shaoling Zhang and Katsuhiro Shiratake and Khanizadeh Shahrokh and Shutian Tao},
journal = {Plant biotechnology journal},
year = {2026},
month = oct,
doi = {10.1111/pbi.70770},
url = {https://europepmc.org/article/MED/42876333},
note = {CC BY},
}
RIS
TY - JOUR
TI - PbSnRK1-Mediated Phosphorylation of PbTCP13 Regulates Glucose-Responsive Lignin Biosynthesis via PbMYB11 During Pear Stone Cell Formation.
AU - Jianan He
AU - Xuxu Wang
AU - Abdul Basit
AU - Wen Li
AU - Jiahui Chao
AU - Wenyu Zhao
AU - Mingxu Niu
AU - Xin Yan
AU - Yuanhui Yu
AU - Kaijie Qi
AU - Zhihua Xie
AU - Shaoling Zhang
AU - Katsuhiro Shiratake
AU - Khanizadeh Shahrokh
AU - Shutian Tao
PY - 2026
DA - 2026/10/15
JO - Plant biotechnology journal
DO - 10.1111/pbi.70770
UR - https://europepmc.org/article/MED/42876333
AB - Stone cell lignification is a key determinant of pear fruit texture and commercial quality, and this process has been reported to be tightly coupled to cellular glucose availability. However, how glucose dose-dependently targets transcription factor phosphorylation during lignin biosynthesis remains largely unknown. Using yeast two-hybrid library screening and phosphorylation assays, we found that PbSnRK1, a glucose-responsive kinase, interacts with and directly phosphorylates PbTCP13, thereby participating in the regulation of stone cell lignification. PbSnRK1 serves as an energy-status sensor linking glucose signalling to biphasic regulation of lignin metabolism in pear. Under low-glucose conditions, activated PbSnRK1 phosphorylates the transcription factor PbTCP13 at Ser265, targeting it for 26S proteasome-mediated degradation and thereby derepressing PbMYB11-PbCCR1 cascade associated with lignin biosynthesis. Under high-glucose conditions, suppressed PbSnRK1 kinase activity results in PbTCP13 protein accumulation, which restricts excessive lignification by both repressing PbCCR1 transcription and physically interacting with PbMYB11 to inhibit its transactivation capacity. This PbSnRK1-PbTCP13-PbMYB11 cascade, balanced by glucose concentration, acts as a molecular switch that activates stone cell formation and lignification at low-glucose levels during early fruit development, while restricting excessive lignification at high-glucose levels during later stages, providing new mechanistic insights into energy-coupled secondary wall metabolism in fleshy fruits.
SN - 1467-7644
SN - 1467-7652
ER -