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TitleN-glycosylation facilitates the activation of a plant cell-surface receptor.
Journal, issue, pagesNat Plants, Vol. 10, Issue 12, Page 2014-2026, Year 2024
Publish dateNov 7, 2024
AuthorsFangshuai Jia / Yu Xiao / Yaojie Feng / Jinghui Yan / Mingzhu Fan / Yue Sun / Shijia Huang / Weiguo Li / Tian Zhao / Zhifu Han / Shuguo Hou / Jijie Chai /
PubMed AbstractPlant receptor kinases (RKs) are critical for transmembrane signalling involved in various biological processes including plant immunity. MALE DISCOVERER1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) is ...Plant receptor kinases (RKs) are critical for transmembrane signalling involved in various biological processes including plant immunity. MALE DISCOVERER1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) is a unique RK that recognizes a family of immunomodulatory peptides called SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) and activates pattern-triggered immunity responses. However, the precise mechanisms underlying SCOOP recognition and activation of MIK2 remain poorly understood. Here we present the cryogenic electron microscopy structure of a ternary complex consisting of the extracellular leucine-rich repeat (LRR) of MIK2 (MIK2LRR), SCOOP12 and the extracellular LRR of the co-receptor BAK1 (BAK1LRR) at a resolution of 3.34 Å. The structure reveals that a DNHH motif in MIK2LRR plays a critical role in specifically recognizing the highly conserved SxS motif of SCOOP12. Furthermore, the structure demonstrates that N-glycans at MIK2LRR directly interact with the N-terminal capping region of BAK1LRR. Mutation of the glycosylation site, MIK2LRR, completely abolishes the SCOOP12-independent interaction between MIK2LRR and BAK1LRR and substantially impairs the assembly of the MIK2LRR-SCOOP12-BAK1LRR complex. Supporting the biological relevance of N410-glycosylation, MIK2 substantially compromises SCOOP12-triggered immune responses in plants. Collectively, these findings elucidate the mechanism underlying the loose specificity of SCOOP recognition by MIK2 and reveal an unprecedented mechanism by which N-glycosylation modification of LRR-RK promotes receptor activation.
External linksNat Plants / PubMed:39511417
MethodsEM (single particle)
Resolution3.34 Å
Structure data

39093

8yaa

EMDB-39093, PDB-8yaa:
Cryo-EM structure of MIK2-SCOOP12-BAK1
Method: EM (single particle) / Resolution: 3.34 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • Arabidopsis (plant)
  • arabidopsis thaliana (thale cress)
KeywordsTRANSFERASE/PLANT PROTEIN / LRR-RLK / SERK / MIK2 / SCOOP / BAK1 / PLANT PROTEIN / TRANSFERASE / PLANT PROTEIN complex / TRANSFERASE-PLANT PROTEIN complex

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