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Peer-reviewedCC BY-NCScience Advances

A phosphorylation-gated GAPDH-MAPK6-LBD1 module controls drought-responsive transcription

  • Zihang He1
  • Zhibo Wang1
  • Caiqiu Gao1
  • Xiaoyu Ji2
  • Yucheng Wang1,2
  1. 1State Key Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin, 150040, China.
  2. 2Shenyang Agricultural University, Shenyang, 110866, China.
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Abstract

Drought adaptation requires rapid spatial reorganization of signaling proteins to reprogram stress-responsive transcription, yet how phosphorylation coordinates this process remains unclear. Here we aimed to define how phosphorylation-gated protein relocalization regulates a BpLBD1-centered drought pathway in Betula platyphylla (birch). Drought activated two kinase branches: BpAGC phosphorylated BpMAPK6 at Ser318 within a cryptic nuclear localization signal, promoting importin α recognition, whereas BpCKII phosphorylated BpGAPDH at Thr109, Thr270, Ser279 and Thr298, promoting importin β recognition. Dual phosphorylation enabled coordinated nuclear accumulation of BpMAPK6 and BpGAPDH. In the nucleus, phosphorylated BpGAPDH acted as a scaffold-like adaptor coupling BpMAPK6 to BpLBD1, enabling BpMAPK6-mediated phosphorylation of BpLBD1 at Ser29. This weakened BpLBD1 binding to the BpMYB123 promoter, reduced expression of the drought-sensitivity regulator BpMYB123, and de-repressed drought-responsive genes such as BpRD29B. Disrupting BpGAPDH or BpLBD1 Ser29 phosphorylation compromised drought tolerance. Thus, a phospho-spatial GAPDH-MAPK6-LBD1 switch couples nuclear protein assembly to drought-responsive transcription.

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Cite

BibTeXRIS
BibTeX
@article{he2026phosphorylationgated,
  title = {{A phosphorylation-gated GAPDH-MAPK6-LBD1 module controls drought-responsive transcription}},
  author = {Zihang He and Zhibo Wang and Caiqiu Gao and Xiaoyu Ji and Yucheng Wang},
  journal = {Science Advances},
  year = {2026},
  month = oct,
  doi = {10.1126/sciadv.aek0125},
  url = {https://www.science.org/doi/10.1126/sciadv.aek0125},
  note = {CC BY-NC},
}
RIS
TY  - JOUR
TI  - A phosphorylation-gated GAPDH-MAPK6-LBD1 module controls drought-responsive transcription
AU  - Zihang He
AU  - Zhibo Wang
AU  - Caiqiu Gao
AU  - Xiaoyu Ji
AU  - Yucheng Wang
PY  - 2026
DA  - 2026/10/21
JO  - Science Advances
DO  - 10.1126/sciadv.aek0125
UR  - https://www.science.org/doi/10.1126/sciadv.aek0125
AB  - Drought adaptation requires rapid spatial reorganization of signaling proteins to reprogram stress-responsive transcription, yet how phosphorylation coordinates this process remains unclear. Here we aimed to define how phosphorylation-gated protein relocalization regulates a BpLBD1-centered drought pathway in Betula platyphylla (birch). Drought activated two kinase branches: BpAGC phosphorylated BpMAPK6 at Ser318 within a cryptic nuclear localization signal, promoting importin α recognition, whereas BpCKII phosphorylated BpGAPDH at Thr109, Thr270, Ser279 and Thr298, promoting importin β recognition. Dual phosphorylation enabled coordinated nuclear accumulation of BpMAPK6 and BpGAPDH. In the nucleus, phosphorylated BpGAPDH acted as a scaffold-like adaptor coupling BpMAPK6 to BpLBD1, enabling BpMAPK6-mediated phosphorylation of BpLBD1 at Ser29. This weakened BpLBD1 binding to the BpMYB123 promoter, reduced expression of the drought-sensitivity regulator BpMYB123, and de-repressed drought-responsive genes such as BpRD29B. Disrupting BpGAPDH or BpLBD1 Ser29 phosphorylation compromised drought tolerance. Thus, a phospho-spatial GAPDH-MAPK6-LBD1 switch couples nuclear protein assembly to drought-responsive transcription.
SN  - 2375-2548
ER  -