Proteomics

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Identification of Endogenous Kinase Substrates by Proximity Labeling Combined with Kinase Perturbation and Phosphorylation Motifs


ABSTRACT: Mass spectrometry-based phosphoproteomics can identify more than 10,000 phosphorylated sites in a single experiment. But, despite the fact that enormous phosphosite information has been accumulated in public repositories, protein kinase-substrate relationships remain largely unknown. Here, we describe a method to identify endogenous substrates of kinases by using a combination of a proximity-dependent biotin identification method, called BioID, with two other independent methods, kinase-perturbed phosphoproteomics and phosphorylation motif matching. For proof-of-concept, this approach was applied to casein kinase 2 (CK2) and protein kinase A (PKA), and identified 33 and 52 putative substrates, respectively. We also show that known cancer-associated missense mutations near phosphosites of substrates affect phosphorylation by CK2 or PKA, and thus might alter downstream signaling in cancer cells bearing these mutations. This approach extends our ability to probe physiological kinase-substrate networks by providing new methodology for large-scale identification of endogenous substrates of kinases.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Yasushi Ishihama 

PROVIDER: PXD019664 | JPOST Repository | Fri Jul 16 00:00:00 BST 2021

REPOSITORIES: jPOST

Dataset's files

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Action DRS
191228TN_02_CX4945_fr1.raw Raw
191228TN_03_CX4945_fr2.raw Raw
191228TN_04_CX4945_fr3.raw Raw
191228TN_05_CX4945_fr4.raw Raw
191228TN_06_CX4945_fr5.raw Raw
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Publications

Identification of Endogenous Kinase Substrates by Proximity Labeling Combined with Kinase Perturbation and Phosphorylation Motifs.

Niinae Tomoya T   Imami Koshi K   Sugiyama Naoyuki N   Ishihama Yasushi Y  

Molecular & cellular proteomics : MCP 20210627


Mass-spectrometry-based phosphoproteomics can identify more than 10,000 phosphorylated sites in a single experiment. But, despite the fact that enormous phosphosite information has been accumulated in public repositories, protein kinase-substrate relationships remain largely unknown. Here, we describe a method to identify endogenous substrates of kinases by using a combination of a proximity-dependent biotin identification method, called BioID, with two other independent methods, kinase-perturbe  ...[more]

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