Proteomics

Dataset Information

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ULK1 phosphorylates and regulates mineralocorticoid receptor

ABSTRACT: To evaluate whether ULK1 phosphorylates mineralocorticoid receptor, we performed in vitro phosphatase assay and determined phosphorylation sites by mass spectrometry.

ORGANISM(S): None

SUBMITTER: Shigeru Shibata 

PROVIDER: PXD010048 | JPOST Repository | Tue Jul 17 00:00:00 BST 2018

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
171110_TEI_MRpeptide_Con_1_5pmol_XL.RAW Raw
171110_TEI_MRpeptide_Ulk_2_5pmol_XL.RAW Raw
Control_F014114.dat Other
ULK1_F014117.dat Other
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Publications

ULK1 Phosphorylates and Regulates Mineralocorticoid Receptor.

Shibata Shigeru S   Ishizawa Kenichi K   Wang Qin Q   Xu Ning N   Fujita Toshiro T   Uchida Shunya S   Lifton Richard P RP  

Cell reports 20180701 3

Mineralocorticoid receptor (MR) signaling regulates both renal Na-Cl reabsorption and K<sup>+</sup> excretion. We previously demonstrated that phosphorylation of S843 in the MR ligand-binding domain in renal intercalated cells is involved in the balance of these activities by regulating ligand binding and signaling. However, the kinase that phosphorylates MR<sup>S843</sup> is unknown. Using a high-throughput screen assay of 197 kinases, we found that ULK1 is the principal kinase that is responsi  ...[more]