Dataset Information

H89 Phosphoproteomics in PKA-Null Cells

ABSTRACT: Protein phosphorylation plays a crucial role in propagating cellular responses to both internal and external cues. One of the most important kinases responsible for protein phosphorylation is protein kinase A (PKA). N-[2-p-bromocinnamylamino-ethyl]-5-isoquinolinesulphonamide (H89) is often used as a “PKA specific inhibitor” to study the involvement of PKA in signaling pathways. However, evidence from cell-free experiments suggested that H89 can also inhibit other kinases. In this experiment, previously-generated mouse collecting duct cell lines with and without PKA were treated with H89, followed by mass spectrometry-based phosphoproteomics to globally assess changes in phosphorylation.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Kavee Limbutara

LAB HEAD: Mark A. Knepper

PROVIDER: PXD011167 | Pride | 2019-03-28

REPOSITORIES: Pride

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Publications

Phosphorylation Changes in Response to Kinase Inhibitor H89 in PKA-Null Cells.

Limbutara Kavee K Kelleher Andrew A Yang Chin-Rang CR Raghuram Viswanathan V Knepper Mark A MA

Scientific reports 20190226 1

Protein phosphorylation, mediated by protein kinases, plays a crucial role in cellular regulation. One of the most important protein kinases is protein kinase A (PKA). N-[2-p-bromocinnamylamino-ethyl]-5-isoquinolinesulphonamide (H89) is often used as a "PKA specific inhibitor" to study the involvement of PKA in signaling pathways. However, evidence from cell-free experiments has suggested that H89 can also inhibit other protein kinases. In this study, previously generated PKA-null and PKA-intact ...[more]

PMID: 30808967

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