4.7 Review

Masks Start to Drop: Suppressor of MAX2 1-Like Proteins Reveal Their Many Faces

期刊

FRONTIERS IN PLANT SCIENCE
卷 13, 期 -, 页码 -

出版社

FRONTIERS MEDIA SA
DOI: 10.3389/fpls.2022.887232

关键词

SMXL; strigolactones; karrikins; phylogenetics; biomolecular condensates

资金

  1. Research Foundation-Flanders [3S015819]
  2. Saclay Plant Sciences-SPS [ANR-17-EUR-0007]
  3. Tournesol (Communaute Flandres-France) program [40660PF]

向作者/读者索取更多资源

This review provides an in-depth exploration of the recent advances in understanding the physiological function, evolution, structure, and molecular mechanism of SUPPRESSOR OF MAX2 1-LIKE (SMXL) proteins. SMXLs regulate various physiological processes in plants, such as shoot and root architecture, seed germination, and seedling photomorphogenesis, through proteasomal degradation. The apparent localization of SMXLs in subnuclear speckles and the potential connection to biomolecular condensates and liquid-liquid phase separation are proposed as future research directions.
Although the main players of the strigolactone (SL) signaling pathway have been characterized genetically, how they regulate plant development is still poorly understood. Of central importance are the SUPPRESSOR OF MAX2 1-LIKE (SMXL) proteins that belong to a family of eight members in Arabidopsis thaliana, of which one subclade is involved in SL signaling and another one in the pathway of the chemically related karrikins. Through proteasomal degradation of these SMXLs, triggered by either DWARF14 (D14) or KARRIKIN INSENSITIVE2 (KAI2), several physiological processes are controlled, such as, among others, shoot and root architecture, seed germination, and seedling photomorphogenesis. Yet another clade has been shown to be involved in vascular development, independently of the D14 and KAI2 actions and not relying on proteasomal degradation. Despite their role in several aspects of plant development, the exact molecular mechanisms by which SMXLs regulate them are not completely unraveled. To fill the major knowledge gap in understanding D14 and KAI2 signaling, SMXLs are intensively studied, making it challenging to combine all the insights into a coherent characterization of these important proteins. To this end, this review provides an in-depth exploration of the recent data regarding their physiological function, evolution, structure, and molecular mechanism. In addition, we propose a selection of future perspectives, focusing on the apparent localization of SMXLs in subnuclear speckles, as observed in transient expression assays, which we couple to recent advances in the field of biomolecular condensates and liquid-liquid phase separation.

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