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ULK1 Phosphorylates and Regulates Mineralocorticoid Receptor

Shibata, Shigeru, Ishizawa, Kenichi, Wang, Qin, Xu, Ning, Fujita, Toshiro, Uchida, Shunya, Lifton, Richard P.·2018·Cell Reports
DOI 10.1016/j.celrep.2018.06.072
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Abstract

Mineralocorticoid receptor (MR) signaling regulates both renal Na-Cl reabsorption and K + 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 S843 is unknown. Using a high-throughput screen assay of 197 kinases, we found that ULK1 is the principal kinase that is responsible for the phosphorylation of MR S843 . The results were confirmed by in vitro kinase assay, mass spectrometry, and siRNA knockdown experiments. Notably, phosphorylation at MR S843 was markedly reduced in ULK1/2 double knockout mouse embryonic fibroblasts. Upstream, we show that ULK1 activity is inhibited by phosphorylation induced by angiotensin II via mTOR in cell culture and in vivo. These findings implicate mTOR and ULK1 as regulators of MR activity in intercalated cells, a pathway that is critical for maintaining electrolyte homeostasis.

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Metadata

Authors
Shibata, S., Ishizawa, K., Wang, Q., Xu, N., Fujita, T., Uchida, S., & Lifton, R. P.
ORCID
Shibata, Shigeru
Venue
Cell Reports
Publisher
Elsevier BV
Published
2018-07
Volume
24
Issue
3
Pages
569-576
ISSN
2211-1247
DOI
10.1016/j.celrep.2018.06.072
Cited by
46
References
2
Language
en
Licence
Funders
  • Japan Society for the Promotion of Science (JSPS) KAKENHI (15H04837, 15H02538)
  • Kanae Foundation for the Promotion of Medical Science
  • Suzuki Memorial Foundation
  • Takeda Science Foundation
  • NIH (P01DK17433)

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