Proteomics

Dataset Information

0

BioID-MS identification of WDR62 binding partners.


ABSTRACT: To identify novel WDR62 binding partners, we generated WDR62 fusion proteins tagged with the BirA* promiscuous biotin ligase. This allowed for spatially restricted biotin labelling, affinity isolation, and detection of proximal proteins and transient interactors within an approximate 10 nm radius of WDR62 through affinity isolation and identificaiton by mass spectrometry.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Early Embryonic Cell

DISEASE(S): Neuroblastoma

SUBMITTER: Dominic Ng  

LAB HEAD: Dominic Chi Hiung Ng

PROVIDER: PXD074147 | Pride | 2026-04-06

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20160113_Yvonne_Y1.group Other
20160113_Yvonne_Y10B.group Other
20160113_Yvonne_Y10B__FDR.xlsx Xlsx
20160113_Yvonne_Y1__FDR.xlsx Xlsx
20160113_Yvonne_Y2.group Other
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Publications

Microcephaly-associated protein WDR62 supports purine metabolism by interacting with co-chaperone BAG2.

Morris Matthew J MJ   Yeap Yvonne Y YY   Edwards Jonathon R JR   Chen Chi C   Paolino Annalisa A   Furness Sebastian G B SGB   Millard S Sean SS   Pagan Julia K JK   Fenlon Laura R LR   Ng Dominic C H DCH  

The EMBO journal 20260305 7


Inherited mutations in the spindle pole-associated scaffold protein WDR62 cause autosomal recessive primary microcephaly. Previous research has characterised the roles of WDR62 in the regulation of spindle dynamics, cell division, and brain development. Here, we identify a new function of this protein in regulating purine metabolism. WDR62 interacts directly with BAG2, a co-chaperone of HSP70/90. Under stress conditions, WDR62 and BAG2 re-localise to cytoplasmic granules enriched for enzymes inv  ...[more]

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