Dataset Information

Dissociation profile of F-box proteins

ABSTRACT: Dissociation rate of different F-box proteins from CUL1 was studied by AP-MS.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Kankan Wang

LAB HEAD: Xing Liu

PROVIDER: PXD045616 | Pride | 2025-01-20

REPOSITORIES: Pride

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			Action	DRS
	2022_03_50_Liu_Kankan_ExplorisFAIMS_HC.pdResult	Other
	2022_03_50_Liu_Kankan_ExplorisFAIMS_HC1.raw	Raw
	2022_03_50_Liu_Kankan_ExplorisFAIMS_HC2.raw	Raw
	2022_03_50_Liu_Kankan_ExplorisFAIMS_HC3.raw	Raw
	2022_03_50_Liu_Kankan_ExplorisFAIMS_LC.pdResult	Other

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Project description:Large-scale studies of protein phosphorylation have generally focused on determining the sites and stoichiometry of phosphorylated proteins derived from different biological specimens such as cell lines and tissue samples. While such information is important for understanding the role of phosphorylation in biological systems, it fails to expose the relationship between protein phosphorylation and protein function. Because of the close link between protein function and protein folding stability, knowledge about phosphorylation-induced protein folding stability changes can lead to a better understanding of the functional effects of protein phosphorylation. As part of this work, the Stability of Proteins from Rate of OXidation (SPROX) and Limited Proteolysis (LiP) techniques were utilized to identify phosphorylation-induced conformational and stability changes in proteins derived from a human breast cancer cell line MCF-7. This was accomplished by comparing the conformation properties of proteins in two MCF-7 cell lysates including one that was and one that was not dephosphorylated with alkaline phosphatase. The SPROX technique, which probes the global unfolding/refolding properties of proteins, identified 168 proteins with phosphorylation-induced stability changes, and the LiPs technique, which probes the more local unfolding/refolding properties of proteins, identified 251 proteins with phosphorylation-induced stability changes. A total of 49 proteins identified here with phosphorylation-induced conformational changes, were previously identified in phosphoproteomic studies to be differentially phosphorlyated in different human breast cancer subtypes. A total of 98 proteins identified here overlapped with protein hits previously found to be differentially stabilized in four human breast cancer phenotypes, suggesting that the phosphorylated changes observed here may be disease related. The experimental approach and results reported here create a novel perspective in understanding large-scale molecular influence of phosphorylation and a shortcut in finding possible functionally significant PTMs in cellular proteins.

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Dissociation profile of F-box proteins

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