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Inline liquid chromatography- Flash oxidation for structural analysis of non-stoichiometric protein-ligand interaction

ABSTRACT: Size exclusion chromatography coupled to a flash oxidation unit from GenNext technologies was used to perform fast photochemical oxidation of proteins of human antithrombin III (ATIII) in the presence of unfractionated heparin. The footprint was calculated for the ATIII alone and ATIII bound to unfractionated heparin.

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ORGANISM(S): Acyrthosiphon Pisum (pea Aphid) Homo Sapiens (human)

SUBMITTER: Sandeep Misra

LAB HEAD: Joshua S. Sharp

PROVIDER: PXD034906 | Pride | 2026-02-02

REPOSITORIES: Pride

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Project description:Cyclin C was cloned as a growth-promoting G1 cyclin1,2, and several studies postulated a role for cyclin C in driving cell proliferation3-8 . Moreover, cyclin C, together with its kinase partner, the cyclin-dependent kinase CDK8, is believed to represent an essential component of basal transcriptional machinery where it globally represses gene expression9-13. However, the function of cyclin C in vivo has never been addressed. Here we show that in the living organism cyclin C acts as a haploinsufficient tumor suppressor, through its function of controlling Notch1 oncogene levels. Cyclin C activates an “orphan” CDK19 kinase14, as well as CDK8 and CDK3. These cyclin C-CDK complexes phosphorylate Notch1 intracellular domain (ICN1), which allows binding of ICN1 to Fbw7 and triggers ICN1 polyubiquitination. Genetic ablation of cyclin C blocks ICN1 phosphorylation, disrupts Fbw7 binding, and decreases ICN1 ubiquitination in vivo, thereby strongly elevating ICN1 levels in several compartments of cyclin C knockout mice. Cyclin C was cloned as a growth-promoting G1 cyclin1,2, and several studies postulated a role for cyclin C in driving cell proliferation3-8 . Moreover, cyclin C, together with its kinase partner, the cyclin-dependent kinase CDK8, is believed to represent an essential component of basal transcriptional machinery where it globally represses gene expression9-13. However, the function of cyclin C in vivo has never been addressed. Here we show that in the living organism cyclin C acts as a haploinsufficient tumor suppressor, through its function of controlling Notch1 oncogene levels. Cyclin C activates an “orphan” CDK19 kinase14, as well as CDK8 and CDK3. These cyclin C-CDK complexes phosphorylate Notch1 intracellular domain (ICN1), which allows binding of ICN1 to Fbw7 and triggers ICN1 polyubiquitination. Genetic ablation of cyclin C blocks ICN1 phosphorylation, disrupts Fbw7 binding, and decreases ICN1 ubiquitination in vivo, thereby strongly elevating ICN1 levels in several compartments of cyclin C knockout mice.

			Action	DRS
	ATIII-LC-FOX1-MSMS.byspec2	Other
	ATIII-LC-FOX1-MSMS.raw	Raw
	ATIII-LC-FOX1.byspec2	Other
	ATIII-LC-FOX1.raw	Raw
	ATIII-LC-FOX2-MSMS.byspec2	Other

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Inline liquid chromatography- Flash oxidation for structural analysis of non-stoichiometric protein-ligand interaction

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