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Corrigendum Free access | 10.1172/JCI83542

Kidney growth and hypertrophy: the role of mTOR and vesicle trafficking

Qais Al-Awqati

Find articles by Al-Awqati, Q. in: JCI | PubMed | Google Scholar

Published August 3, 2015 - More info

Published in Volume 125, Issue 8 on August 3, 2015
J Clin Invest. 2015;125(8):3304–3304. https://doi.org/10.1172/JCI83542.
Copyright © 2015, American Society for Clinical Investigation
Published August 3, 2015 - Version history
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Kidney growth and hypertrophy: the role of mTOR and vesicle trafficking
Qais Al-Awqati
Qais Al-Awqati
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Kidney growth and hypertrophy: the role of mTOR and vesicle trafficking

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Abstract

The kidney, like other organs, grows in constant proportion to the rest of the body. When one kidney is removed, the remaining one hypertrophies. In a comprehensive series of studies, Chen et al. show that growth during maturation is mediated by the mTORC1 signaling pathway, which is induced by EGF-like peptides, and requires PI3K, PDK, AKT, mTORC2, and activation of mTORC1 through the combined effects of TSC and RHEB as part of a multiprotein complex localized on lysosomes. However, compensatory growth is mediated by amino acids, which act on mTORC1 independently of the previous pathway, and requires a class III PI3K (VPS34) that is known to be involved in vesicle trafficking to the lysosomes.

Authors

Qais Al-Awqati

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Original citation: J Clin Invest. 2015;125(6):2267–2270. doi:10.1172/JCI81508.

Citation for this corrigendum: J Clin Invest. 2015;125(8):3304. doi:10.1172/JCI83542.

Two sentences were incorrect in the original manuscript. The first appeared in the section titled “Increased amino acid delivery causes compensatory hypertrophy.” The second appeared in the legend for Figure 1. The correct two sentences are below.

Once the mTORC1-containing complex is recruited to the lysosome, it encounters RHEB, whose inhibition activates it.

mTORC1 is recruited into a large protein complex on the lysosome surface composed of RAG GTPase, Ragulator, V-ATPase, and the amino acid transporter SLC38A9, allowing mTORC1 to be activated via inhibition of RHEB.

The author regrets the errors.

Footnotes

See the related article beginning on page 2267.

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