Abstract
Main conclusion
The N-myristoylation is required for BSK1 proper plasma membrane targeting and protein turnover.
Abstract
Brassinosteroid (BR) signaling kinase 1 (BSK1), with a myristoylation site at its N-terminus to anchor at plasma membrane (PM), is involved in BR-regulated plant growth and flg22-triggered immunity responses. However, little is known about the role of N-myristoylation in BSK1 protein homeostasis. Here, we revealed that N-myristoylation is critical to the PM targeting and protein stability of BSK1. The N-myristoylation-deficient mutant BSK1G2A mainly distributed in the cytoplasm and retained in the endoplasmic reticulum. We further found that the BSK1G2A proteins were unstable and degraded through ATG8e-labled autophagic pathway. This study provides a new insight into the regulation of plant protein homeostasis.
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Data availability
Data sharing not applicable to this article as no datasets were generated or analyzed during the current study.
Abbreviations
- BFA:
-
Brefeldin A
- BR:
-
Brassinosteroid
- BSK1:
-
BR signaling kinase 1
- ER:
-
Endoplasmic reticulum
- HDEL:
-
His–Asp–Glu–Leu
- PM:
-
Plasma membrane
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Acknowledgements
We thank Prof. Dingzhong Tang for providing plasmid BSK1G2A-GFP, and Prof. Xueping Zhou for providing plasmids RFP-HEDL and RFP-ATG8e. This work is supported by the National Natural Science Foundation of China (31871424) and China Postdoctoral Science Foundation (2021M701922).
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Su, B., Wang, A. & Shan, X. The role of N-myristoylation in homeostasis of brassinosteroid signaling kinase 1. Planta 255, 73 (2022). https://doi.org/10.1007/s00425-022-03861-y
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DOI: https://doi.org/10.1007/s00425-022-03861-y