Dataset Information

An N-glycan on the C2 domain of Jagged-1 is essential for Notch activation

ABSTRACT: Glycoproteomics determination of human jagged-1 glycan composition

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Sean Burnap

LAB HEAD: Weston Struwe

PROVIDER: PXD034133 | Pride | 2022-10-17

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	KO_Alpha_HCD.raw	Raw
	KO_Alpha_HCD.raw_20220509_Byonic.byrslt	Raw
	KO_Chym_HCD.raw	Raw
	KO_Chym_HCD.raw_20220509_Byonic.byrslt	Raw
	KO_Tryp_HCD.raw	Raw

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Publications

An N-glycan on the C2 domain of JAGGED1 is important for Notch activation.

Meng Yao Y Sanlidag Sami S Jensen Sacha A SA Burnap Sean A SA Struwe Weston B WB Larsen Andreas H AH Feng Xinyi X Mittal Shruti S Sansom Mark S P MSP Sahlgren Cecilia C Handford Penny A PA

Science signaling 20221011 755

The canonical members of the Jagged/Serrate and Delta families of transmembrane ligands have an extracellular, amino-terminal C2 domain that binds to phospholipids and is required for optimal activation of the Notch receptor. Somatic mutations that cause amino substitutions in the C2 domain in human JAGGED1 (JAG1) have been identified in tumors. We found in reporter cell assays that mutations affecting an N-glycosylation site reduced the ligand's ability to activate Notch. This N-glycosylation s ...[more]

PMID: 36219682

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