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Related Experiment Video

Updated: Jun 14, 2026

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments

Published on: July 5, 2014

mTOR complex-2 activates ENaC by phosphorylating SGK1.

Ming Lu¹, Jian Wang, Kevin T Jones

¹Department of Medicine, University of California, San Francisco, San Francisco, CA 94107, USA.

Journal of the American Society of Nephrology : JASN

|March 27, 2010

Summary

This summary is machine-generated.

Mammalian target of rapamycin (mTOR), specifically mTORC2, phosphorylates serum- and glucocorticoid-induced kinase 1 (SGK1), activating epithelial sodium channel (ENaC) and regulating sodium transport in the kidney. This identifies the key kinase for SGK1 activity.

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Area of Science:

Biochemistry
Molecular Biology
Physiology

Background:

Serum- and glucocorticoid-induced kinase 1 (SGK1) is crucial for regulating sodium transport in the kidney's distal nephron.
SGK1 activity is controlled by phosphorylation of its hydrophobic motif (HM), but the responsible kinase was unidentified.

Purpose of the Study:

To identify the kinase responsible for phosphorylating the hydrophobic motif of SGK1.
To determine the role of this kinase in activating SGK1 and regulating epithelial sodium channel (ENaC)-dependent sodium transport.

Main Methods:

Utilized co-immunoprecipitation to assess interactions between SGK1, mTOR, rictor, and raptor.
Employed small hairpin RNA (shRNA) to knock down rictor and raptor expression.
Inhibited mTOR and mTORC1 complexes to evaluate effects on SGK1 phosphorylation and ENaC activity.

Main Results:

Mammalian target of rapamycin (mTOR), complexed with rictor (forming mTORC2), directly phosphorylates SGK1's hydrophobic motif.
mTORC2-mediated SGK1 phosphorylation is essential for activating ENaC and facilitating sodium transport.
mTORC1, in contrast, does not phosphorylate SGK1 or influence ENaC activity.

Conclusions:

mTORC2 is identified as the hydrophobic motif kinase for SGK1.
This finding elucidates a critical step in the regulation of sodium balance, highlighting mTORC2's role in ENaC-dependent sodium transport.