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Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

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Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. / Tan, Minjia; Peng, Chao; Anderson, Kristin A; Chhoy, Peter; Xie, Zhongyu; Dai, Lunzhi; Park, Jeongsoon; Chen, Yue; Huang, He; Zhang, Yi; Ro, Jennifer; Wagner, Gregory R; Green, Michelle F; Madsen, Andreas S; Schmiesing, Jessica; Peterson, Brett S; Xu, Guofeng; Ilkayeva, Olga R; Muehlbauer, Michael J; Braulke, Thomas; Mühlhausen, Chris; Backos, Donald S; Olsen, Christian A; McGuire, Peter J; Pletcher, Scott D; Lombard, David B; Hirschey, Matthew D; Zhao, Yingming.

in: CELL METAB, Jahrgang 19, Nr. 4, 01.04.2014, S. 605-17.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Tan, M, Peng, C, Anderson, KA, Chhoy, P, Xie, Z, Dai, L, Park, J, Chen, Y, Huang, H, Zhang, Y, Ro, J, Wagner, GR, Green, MF, Madsen, AS, Schmiesing, J, Peterson, BS, Xu, G, Ilkayeva, OR, Muehlbauer, MJ, Braulke, T, Mühlhausen, C, Backos, DS, Olsen, CA, McGuire, PJ, Pletcher, SD, Lombard, DB, Hirschey, MD & Zhao, Y 2014, 'Lysine glutarylation is a protein posttranslational modification regulated by SIRT5', CELL METAB, Jg. 19, Nr. 4, S. 605-17. https://doi.org/10.1016/j.cmet.2014.03.014

APA

Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., Ro, J., Wagner, G. R., Green, M. F., Madsen, A. S., Schmiesing, J., Peterson, B. S., Xu, G., Ilkayeva, O. R., Muehlbauer, M. J., ... Zhao, Y. (2014). Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. CELL METAB, 19(4), 605-17. https://doi.org/10.1016/j.cmet.2014.03.014

Vancouver

Tan M, Peng C, Anderson KA, Chhoy P, Xie Z, Dai L et al. Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. CELL METAB. 2014 Apr 1;19(4):605-17. https://doi.org/10.1016/j.cmet.2014.03.014

Bibtex

@article{ca46eeb4cb5043898c154cb34595b474,
title = "Lysine glutarylation is a protein posttranslational modification regulated by SIRT5",
abstract = "We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine glutarylation (Kglu). This protein modification was detected by immunoblot and mass spectrometry (MS), and then comprehensively validated by chemical and biochemical methods. We demonstrated that the previously annotated deacetylase, sirtuin 5 (SIRT5), is a lysine deglutarylase. Proteome-wide analysis identified 683 Kglu sites in 191 proteins and showed that Kglu is highly enriched on metabolic enzymes and mitochondrial proteins. We validated carbamoyl phosphate synthase 1 (CPS1), the rate-limiting enzyme in urea cycle, as a glutarylated protein and demonstrated that CPS1 is targeted by SIRT5 for deglutarylation. We further showed that glutarylation suppresses CPS1 enzymatic activity in cell lines, mice, and a model of glutaric acidemia type I disease, the last of which has elevated glutaric acid and glutaryl-CoA. This study expands the landscape of lysine acyl modifications and increases our understanding of the deacylase SIRT5.",
author = "Minjia Tan and Chao Peng and Anderson, {Kristin A} and Peter Chhoy and Zhongyu Xie and Lunzhi Dai and Jeongsoon Park and Yue Chen and He Huang and Yi Zhang and Jennifer Ro and Wagner, {Gregory R} and Green, {Michelle F} and Madsen, {Andreas S} and Jessica Schmiesing and Peterson, {Brett S} and Guofeng Xu and Ilkayeva, {Olga R} and Muehlbauer, {Michael J} and Thomas Braulke and Chris M{\"u}hlhausen and Backos, {Donald S} and Olsen, {Christian A} and McGuire, {Peter J} and Pletcher, {Scott D} and Lombard, {David B} and Hirschey, {Matthew D} and Yingming Zhao",
note = "Copyright {\textcopyright} 2014 Elsevier Inc. All rights reserved.",
year = "2014",
month = apr,
day = "1",
doi = "10.1016/j.cmet.2014.03.014",
language = "English",
volume = "19",
pages = "605--17",
journal = "CELL METAB",
issn = "1550-4131",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

AU - Tan, Minjia

AU - Peng, Chao

AU - Anderson, Kristin A

AU - Chhoy, Peter

AU - Xie, Zhongyu

AU - Dai, Lunzhi

AU - Park, Jeongsoon

AU - Chen, Yue

AU - Huang, He

AU - Zhang, Yi

AU - Ro, Jennifer

AU - Wagner, Gregory R

AU - Green, Michelle F

AU - Madsen, Andreas S

AU - Schmiesing, Jessica

AU - Peterson, Brett S

AU - Xu, Guofeng

AU - Ilkayeva, Olga R

AU - Muehlbauer, Michael J

AU - Braulke, Thomas

AU - Mühlhausen, Chris

AU - Backos, Donald S

AU - Olsen, Christian A

AU - McGuire, Peter J

AU - Pletcher, Scott D

AU - Lombard, David B

AU - Hirschey, Matthew D

AU - Zhao, Yingming

N1 - Copyright © 2014 Elsevier Inc. All rights reserved.

PY - 2014/4/1

Y1 - 2014/4/1

N2 - We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine glutarylation (Kglu). This protein modification was detected by immunoblot and mass spectrometry (MS), and then comprehensively validated by chemical and biochemical methods. We demonstrated that the previously annotated deacetylase, sirtuin 5 (SIRT5), is a lysine deglutarylase. Proteome-wide analysis identified 683 Kglu sites in 191 proteins and showed that Kglu is highly enriched on metabolic enzymes and mitochondrial proteins. We validated carbamoyl phosphate synthase 1 (CPS1), the rate-limiting enzyme in urea cycle, as a glutarylated protein and demonstrated that CPS1 is targeted by SIRT5 for deglutarylation. We further showed that glutarylation suppresses CPS1 enzymatic activity in cell lines, mice, and a model of glutaric acidemia type I disease, the last of which has elevated glutaric acid and glutaryl-CoA. This study expands the landscape of lysine acyl modifications and increases our understanding of the deacylase SIRT5.

AB - We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine glutarylation (Kglu). This protein modification was detected by immunoblot and mass spectrometry (MS), and then comprehensively validated by chemical and biochemical methods. We demonstrated that the previously annotated deacetylase, sirtuin 5 (SIRT5), is a lysine deglutarylase. Proteome-wide analysis identified 683 Kglu sites in 191 proteins and showed that Kglu is highly enriched on metabolic enzymes and mitochondrial proteins. We validated carbamoyl phosphate synthase 1 (CPS1), the rate-limiting enzyme in urea cycle, as a glutarylated protein and demonstrated that CPS1 is targeted by SIRT5 for deglutarylation. We further showed that glutarylation suppresses CPS1 enzymatic activity in cell lines, mice, and a model of glutaric acidemia type I disease, the last of which has elevated glutaric acid and glutaryl-CoA. This study expands the landscape of lysine acyl modifications and increases our understanding of the deacylase SIRT5.

U2 - 10.1016/j.cmet.2014.03.014

DO - 10.1016/j.cmet.2014.03.014

M3 - SCORING: Journal article

C2 - 24703693

VL - 19

SP - 605

EP - 617

JO - CELL METAB

JF - CELL METAB

SN - 1550-4131

IS - 4

ER -