Proteomics

Dataset Information

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Phos-tag SDS-PAGE followed by LC-MS/MS analysis of in vitro phosphorylated Nab2, Foxk1, and HURP

ABSTRACT: Purified GST-fused Nab2, Foxk1, and HURP were incubated with ATP in the presence or absence of His-tagged active ERK in vitro, separated by Phos-tag SDS-PAGE, and visualized by CBB staining. The most shifted regions of protein bands on the Phos-tag-containing gels were excised, digested with trypsin, and analyzed by LC-MS/MS.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Hidetaka Kosako 

PROVIDER: PXD028837 | JPOST Repository | Thu Mar 03 00:00:00 GMT 2022

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
92_Yoshikawa_1_Foxk1_10ng_Ingel_Phos_Tag_QEp.pdResult Other
92_Yoshikawa_1_Foxk1_10ng_Ingel_Phos_Tag_QEp.raw Raw
94_Yoshikawa_2_Nab2_50ng_Ingel_Phos_Tag_QEp.pdResult Other
94_Yoshikawa_2_Nab2_50ng_Ingel_Phos_Tag_QEp.raw Raw
96_Yoshikawa_3_HURP_top_10ng_Ingel_Phos_Tag_QEp.pdResult Other
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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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