Proteomics

Dataset Information

0

PHD3 and FIH substrates cluster in distinct signalling pathways


ABSTRACT: Amino acid hydroxylation is a common post-translational modification which regulates intra and inter-molecular protein-protein interactions. The modifications are regulated by a family of 2-oxoglutarate (2OG) dependent enzymes and although the biochemistry is well understood, until now only a few substrates have been described for these enzymes. We present here a sensitive method which specifically enriches and identifies hydroxylase substrates. We screened for substrates of PHD3 and FIH, a proline and asparagine hydroxylase respectively which regulate the HIF-mediated hypoxic response and were able to confirm known substrates as well as identifying hundreds of potential novel ones. Enrichment analysis revealed that the substrates of both hydroxylases cluster in the same pathways but frequently modify different nodes of these networks. We confirm that two proteins identified in this screen, MAPK6 and RIPK4, are indeed hydroxylated in a FIH or PHD3 dependent mechanism and explore the biological consequences of the hydroxylation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Alex von kriegsheim  

LAB HEAD: Alex von Kriegsheim

PROVIDER: PXD001085 | Pride | 2016-03-30

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
031513_JRM_1.raw Raw
031513_JRM_10.raw Raw
031513_JRM_10_130328182545.raw Raw
031513_JRM_11.raw Raw
031513_JRM_11_130328193316.raw Raw
Items per page:
1 - 5 of 61
altmetric image

Publications

Substrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling Pathways.

Rodriguez Javier J   Pilkington Ruth R   Garcia Munoz Amaya A   Nguyen Lan K LK   Rauch Nora N   Kennedy Susan S   Monsefi Naser N   Herrero Ana A   Taylor Cormac T CT   von Kriegsheim Alex A  

Cell reports 20160310 11


Amino acid hydroxylation is a post-translational modification that regulates intra- and inter-molecular protein-protein interactions. The modifications are regulated by a family of 2-oxoglutarate- (2OG) dependent enzymes and, although the biochemistry is well understood, until now only a few substrates have been described for these enzymes. Using quantitative interaction proteomics, we screened for substrates of the proline hydroxylase PHD3 and the asparagine hydroxylase FIH, which regulate the  ...[more]

Similar Datasets

2016-01-11 | PXD002103 | Pride
2017-03-29 | MSV000080766 | MassIVE
2019-07-09 | PXD011252 | Pride
2020-03-23 | PXD013116 | Pride
2022-08-11 | PXD017278 | Pride
2016-10-25 | E-MTAB-4264 | biostudies-arrayexpress
2016-08-31 | E-MTAB-4300 | biostudies-arrayexpress
2024-09-02 | BIOMD0000000300 | BioModels
2017-03-28 | MSV000080695 | MassIVE
2019-10-09 | GSE136414 | GEO