PXD054177-1

PXD054177 is an original dataset announced via ProteomeXchange.

Title	N-glycosylation facilitates the activation of a plant cell-surface receptor
Description	Plant receptor kinases (RKs) are critical for transmembrane signaling 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 (PTI) responses. However, the precise mechanisms underlying SCOOP recognition and activation of MIK2 remain poorly understood. In this study, we present the cryo-EM structure of a ternary complex consisting of the extracellular leucine-rich repeat 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 MIK2LRRAsn410 directly interact with the N-terminal capping region of BAK1LRR. Mutation of the glycosylation site, MIK2LRRN410D, completely abolishes the SCOOP12-independent interaction between MIK2LRR and BAK1LRR and significantly impairs the assembly of the MIK2LRR-SCOOP12-BAK1LRR complex. Supporting the biological relevance of N410-glycosylation, MIK2N410D 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.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-21_18:48:20.283.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Fangshuai Jia
SpeciesList	scientific name: Trichoplusia ni; NCBI TaxID: 7111;
ModificationList	Hex9HexNAc2 N4-glycosylated asparagine
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2024-07-24 05:39:05	ID requested
⏵ 1	2024-10-21 18:48:20	announced

10.1038/S41477-024-01841-6;

submitter keyword: N-glycosylation，MIK2LRR

Jijie Chai
contact affiliation	Westlake University
contact email	chaijijie@westlake.edu.cn
lab head
Fangshuai Jia
contact affiliation	Henan Normal University
contact email	jiafangshuai@stu.htu.edu.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD054177
     1. Label: PRIDE project
     2. Name: N-glycosylation facilitates the activation of a plant cell-surface receptor