<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Mandalasi MN</submitter><funding>National Institute of Allergy and Infectious Diseases</funding><funding>National Institute of Allergy and Infectious Diseases Division of Intramural Research</funding><funding>NIAID NIH HHS</funding><funding>National Institutes of Health</funding><pagination>107801</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11570480</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>300(11)</volume><pubmed_abstract>A dynamic proteome is required for cellular adaption to changing environments including levels of O&lt;sub>2&lt;/sub>, and the SKP1/CULLIN-1/F-box protein/RBX1 (SCF) family of E3 ubiquitin ligases contributes importantly to proteasome-mediated degradation. We examine, in the apicomplexan parasite Toxoplasma gondii, the influence on the interactome of SKP1 by its novel glycan attached to hydroxyproline generated by PHYa, the likely ortholog of the HIFα PHD2 oxygen-sensor of human host cells. Strikingly, the representation of several putative F-box proteins (FBPs) is substantially reduced in PHYaΔ parasites grown in fibroblasts. One, FBXO13, is a predicted lysyl hydroxylase related to the human JmjD6 oncogene except for its F-box domain. The abundance of FBXO13, epitope-tagged at its genetic locus</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Oxygen-dependent regulation of F-box proteins in Toxoplasma gondii is mediated by Skp1 glycosylation.</pubmed_title><pmcid>PMC11570480</pmcid><funding_grant_id>R01 AI150240</funding_grant_id><funding_grant_id>R01-AI150240</funding_grant_id><funding_grant_id>R01 AI169849</funding_grant_id><funding_grant_id>R21-AI149405</funding_grant_id><funding_grant_id>T32 AI060546</funding_grant_id><funding_grant_id>T32-AI060546</funding_grant_id><funding_grant_id>R21 AI149405</funding_grant_id><pubmed_authors>Deng B</pubmed_authors><pubmed_authors>Mandalasi MN</pubmed_authors><pubmed_authors>Boons GJ</pubmed_authors><pubmed_authors>Baptista CG</pubmed_authors><pubmed_authors>West CM</pubmed_authors><pubmed_authors>Gas-Pascual E</pubmed_authors><pubmed_authors>Kruijtzer JAW</pubmed_authors><pubmed_authors>van der Wel H</pubmed_authors><pubmed_authors>Blader IJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>Oxygen-dependent regulation of F-box proteins in Toxoplasma gondii is mediated by Skp1 glycosylation.</name><description>A dynamic proteome is required for cellular adaption to changing environments including levels of O&lt;sub>2&lt;/sub>, and the SKP1/CULLIN-1/F-box protein/RBX1 (SCF) family of E3 ubiquitin ligases contributes importantly to proteasome-mediated degradation. We examine, in the apicomplexan parasite Toxoplasma gondii, the influence on the interactome of SKP1 by its novel glycan attached to hydroxyproline generated by PHYa, the likely ortholog of the HIFα PHD2 oxygen-sensor of human host cells. Strikingly, the representation of several putative F-box proteins (FBPs) is substantially reduced in PHYaΔ parasites grown in fibroblasts. One, FBXO13, is a predicted lysyl hydroxylase related to the human JmjD6 oncogene except for its F-box domain. The abundance of FBXO13, epitope-tagged at its genetic locus</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Nov</publication><modification>2026-05-26T14:00:18.837Z</modification><creation>2025-04-21T21:45:11.435Z</creation></dates><accession>S-EPMC11570480</accession><cross_references><pubmed>39307307</pubmed><doi>10.1016/j.jbc.2024.107801</doi></cross_references></HashMap>