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- W4384069571 abstract "Protein post-translational modifications (PTMs), such as ubiquitination, phosphorylation, and SUMOylation, are crucial for regulating protein stability, activity, subcellular localization, and binding with cofactors. Such modifications remarkably increase the variety and complexity of proteomes, which are essential for regulating numerous cellular and physiological processes. The regulation of auxin signaling is finely tuned in time and space to guide various plant growth and development. Accumulating evidence indicates that PTMs play critical roles in auxin signaling regulations. Thus, a thorough and systematic review of the functions of PTMs in auxin signal transduction will improve our profound comprehension of the regulation mechanism of auxin signaling and auxin-mediated various processes. This review discusses the progress of protein ubiquitination, phosphorylation, histone acetylation and methylation, SUMOylation, and S-nitrosylation in the regulation of auxin signaling." @default.
- W4384069571 created "2023-07-13" @default.
- W4384069571 creator A5012547855 @default.
- W4384069571 creator A5017100408 @default.
- W4384069571 creator A5050930851 @default.
- W4384069571 creator A5069524933 @default.
- W4384069571 creator A5082631773 @default.
- W4384069571 creator A5087915363 @default.
- W4384069571 date "2023-07-01" @default.
- W4384069571 modified "2023-10-16" @default.
- W4384069571 title "Protein post-translational modifications in auxin signaling" @default.
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