The picky mTORC1 in metabolic enzyme degradation

Yujin Chun; David A Fruman; Gina Lee

doi:10.1016/j.molcel.2024.05.013

The picky mTORC1 in metabolic enzyme degradation

Mol Cell. 2024 Jun 6;84(11):2011-2013. doi: 10.1016/j.molcel.2024.05.013.

Authors

Yujin Chun¹, David A Fruman², Gina Lee³

Affiliations

¹ Department of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, Irvine, CA, USA.
² Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of California, Irvine, Irvine, CA, USA; Chao Family Comprehensive Cancer Center, University of California, Irvine, Irvine, CA, USA.
³ Department of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, Irvine, CA, USA; Chao Family Comprehensive Cancer Center, University of California, Irvine, Irvine, CA, USA. Electronic address: ginalee@uci.edu.

PMID: 38848689
DOI: 10.1016/j.molcel.2024.05.013

Abstract

In this issue of Molecular Cell, Yi et al.¹ demonstrate that reduced mTORC1 activity induces the CTLH E3 ligase-dependent degradation of HMGCS1, an enzyme in the mevalonate pathway, thus revealing a unique connection between mTORC1 signaling and the degradation of a specific metabolic enzyme via the ubiquitin-proteasome system.

MeSH terms

Animals
Humans
Mechanistic Target of Rapamycin Complex 1* / genetics
Mechanistic Target of Rapamycin Complex 1* / metabolism
Mevalonic Acid / metabolism
Multiprotein Complexes / genetics
Multiprotein Complexes / metabolism
Proteasome Endopeptidase Complex* / metabolism
Proteolysis
Signal Transduction*
TOR Serine-Threonine Kinases / genetics
TOR Serine-Threonine Kinases / metabolism
Ubiquitin / metabolism
Ubiquitin-Protein Ligases / genetics
Ubiquitin-Protein Ligases / metabolism

Substances

Mechanistic Target of Rapamycin Complex 1
Proteasome Endopeptidase Complex
Ubiquitin-Protein Ligases
TOR Serine-Threonine Kinases
Multiprotein Complexes
Mevalonic Acid
Ubiquitin