Proteomics

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PRM analysis of phosphopeptides of Nab2, Foxk1, HURP, ERK1/2, NPM, and Hspa4 from ΔB-Raf:ER cells.

ABSTRACT: ΔB-Raf:ER cells were treated with U0126 or 4-HT for 30 min in four biological replicates. Total proteins from cell lysates were digested with Typsin/Lys-C mix, and phosphopeptides were enriched by IMAC using Fe-NTA columns. After data-dependent LC-MS/MS analysis, phosphopeptides of Nab2, Foxk1, HURP, ERK1/2, NPM, and Hspa4 were selected and quantified by targeted MS using the PRM method. Targeted MS/MS scans were acquired by a time-scheduled inclusion list at a resolution of 70,000, an AGC target of 2e5, an isolation window of 2.0 m/z, a maximum injection time of 500 ms, and a normalized collision energy of 27. Time alignment and relative quantification of the transitions were performed using Skyline software.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Hidetaka Kosako 

PROVIDER: PXD028826 | JPOST Repository | Thu Mar 03 00:00:00 GMT 2022

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
41_BRaf_U1_Fe_PRM_180min_QEp.raw Raw
43_BRaf_HT1_Fe_PRM_180min_QEp.raw Raw
45_BRaf_U2_Fe_PRM_180min_QEp.raw Raw
47_BRaf_HT2_Fe_PRM_180min_QEp.raw Raw
49_BRaf_U3_Fe_PRM_180min_QEp.raw Raw
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Publications

Identification and validation of new ERK substrates by phosphoproteomic technologies including Phos-tag SDS-PAGE.

Yoshikawa Harunori H   Nishino Kohei K   Kosako Hidetaka H  

Journal of proteomics 20220226

The extracellular signal-regulated kinase (ERK), a member of the mitogen-activated protein (MAP) kinase family, governs various cellular processes by phosphorylating a large set of substrates. Although many studies have expanded the number of ERK substrates, it is likely that additional substrates remain to be discovered. Here we have employed a quantitative phosphoproteomic approach to explore novel ERK substrates in NIH3T3 fibroblasts stably expressing a fusion protein between B-Raf and estrog  ...[more]

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