4.8 Article

DYNAMIN-RELATED PROTEIN DRP1A functions with DRP2B in plant growth, flg22-immune responses, and endocytosis

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PLANT PHYSIOLOGY
卷 185, 期 4, 页码 1986-2002

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OXFORD UNIV PRESS INC
DOI: 10.1093/plphys/kiab024

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资金

  1. National Science Foundation [(NSF)-IOS 1147032, NSF-IOS 1025837, NSF-GRF 1443129, NSF-MCB 1121998, NSF-MCB 1614915]
  2. National Institute of Health (NIH)-Initiative Maximizing Student Diversity (IMSD) Fellowship [R25 GM056901]
  3. University of Missouri(MU)-Diane P. and Robert E. Sharp Fund Fellowship
  4. Daniel F. Millikan Graduate Fellowship (MU-Division of Plant Sciences)
  5. MU-College of Agriculture, Natural Food and Resources-Undergraduate Research Internship
  6. Dudley Alexander Undergraduate Research OnCampus Internships Gift Fund
  7. MU-Discovery Fellowship
  8. MU-Life Sciences Undergraduate Research Opportunity Fellowship

向作者/读者索取更多资源

The study identified the critical role of Arabidopsis DRP1A in ligand-induced endocytosis of FLS2 and its physiological functions in bacterial immune responses. It also revealed the synergistic roles of DRP1A and DRP2B in plant growth, mutant phenotypes, and PM regulation of FLS2. The study suggests the importance of DRP1A and DRP2B in maintaining proper levels of FLS2 for distinct flg22 responses by potentially modulating the lipid environment in specific PM domains.
Ligand-induced endocytosis of the immune receptor FLAGELLIN SENSING2 (FLS2) is critical for maintaining its proper abundance in the plasma membrane (PM) to initiate and subsequently down regulate cellular immune responses to bacterial flagellin or flg22-peptide. The molecular components governing PM abundance of FLS2, however, remain mostly unknown. Here, we identified Arabidopsis (Arabidopsis thaliana) DYNAMIN-RELATED PROTEIN1A (DRP1A), a member of a plant-specific family of large dynamin GTPases, as a critical contributor to ligand-induced endocytosis of FLS2 and its physiological roles in flg22-signaling and immunity against Pseudomonas syringae pv. tomato DC3000 bacteria in leaves. Notably, drp1a single mutants displayed similar flg22-defects as those previously reported for mutants in another dynamin-related protein, DRP2B, that was previously shown to colocalize with DRP1A. Our study also uncovered synergistic roles of DRP1A and DRP2B in plant growth and development as drp1a drp2b double mutants exhibited severely stunted roots and cotyledons, as well as defective cell shape, cytokinesis, and seedling lethality. Furthermore, drp1a drp2b double mutants hyperaccumulated FLS2 in the PM prior to flg22-treatment and exhibited a block in ligand-induced endocytosis of FLS2, indicating combinatorial roles for DRP1A and DRP1B in governing PM abundance of FLS2. However, the increased steady-state PM accumulation of FLS2 in drp1a drp2b double mutants did not result in increased flg22 responses. We propose that DRP1A and DRP2B are important for the regulation of PM-associated levels of FLS2 necessary to attain signaling competency to initiate distinct flg22 responses, potentially through modulating the lipid environment in defined PM domains.

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