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Molecular & Cellular Oncology Volume 7, 2020 - Issue 3
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Commentary

Lysine succinylation and SIRT5 couple nutritional status to glutamine catabolism

Michael J. LukeyDepartment of Molecular Medicine, Cornell University, Ithaca, NY, USA;Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, USAORCID Iconhttps://orcid.org/0000-0003-3608-3883View further author information
ORCID Icon,
Kai Su GreeneDepartment of Molecular Medicine, Cornell University, Ithaca, NY, USAView further author information
&
Richard A. CerioneDepartment of Molecular Medicine, Cornell University, Ithaca, NY, USACorrespondence[email protected]
View further author information
Article: 1735284 | Received 12 Feb 2020, Accepted 20 Feb 2020, Published online: 19 Mar 2020

Figures & data

Figure 1. Lysine succinylation and sirtuin 5 (SIRT5) connect nutrient availability to metabolic flux. Glutaminase (GLS) initiates the conversion of glutamine to α-ketoglutarate (α-KG) for tricarboxylic acid (TCA) cycle anaplerosis. Reaction of the TCA cycle intermediate succinyl-CoA with lysine K164 on GLS tags it for ubiquitination (at residue K158) and subsequent degradation. SIRT5 stabilizes GLS by catalyzing the desuccinylation of K164, a reaction which requires nicotinamide adenine dinucleotide (NAD+) as a co-substrate.

Figure 1. Lysine succinylation and sirtuin 5 (SIRT5) connect nutrient availability to metabolic flux. Glutaminase (GLS) initiates the conversion of glutamine to α-ketoglutarate (α-KG) for tricarboxylic acid (TCA) cycle anaplerosis. Reaction of the TCA cycle intermediate succinyl-CoA with lysine K164 on GLS tags it for ubiquitination (at residue K158) and subsequent degradation. SIRT5 stabilizes GLS by catalyzing the desuccinylation of K164, a reaction which requires nicotinamide adenine dinucleotide (NAD+) as a co-substrate.

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