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Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. / Colak, Gozde; Pougovkina, Olga; Dai, Lunzhi et al.

In: Molecular & cellular proteomics, Vol. 14, No. 11, 2015, p. 3056-3071.

Research output: Contribution to journal › Article › Academic › peer-review

Harvard

Colak, G, Pougovkina, O, Dai, L, Tan, M, te Brinke, H, Huang, H, Cheng, Z, Park, J, Wan, X, Liu, X, Yue, WW, Wanders, RJA, Locasale, JW, Lombard, DB, de Boer, VCJ & Zhao, Y 2015, 'Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation', Molecular & cellular proteomics, vol. 14, no. 11, pp. 3056-3071. https://doi.org/10.1074/mcp.M115.048850

APA

Colak, G., Pougovkina, O., Dai, L., Tan, M., te Brinke, H., Huang, H., Cheng, Z., Park, J., Wan, X., Liu, X., Yue, W. W., Wanders, R. J. A., Locasale, J. W., Lombard, D. B., de Boer, V. C. J., & Zhao, Y. (2015). Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Molecular & cellular proteomics, 14(11), 3056-3071. https://doi.org/10.1074/mcp.M115.048850

Vancouver

Colak G, Pougovkina O, Dai L, Tan M, te Brinke H, Huang H et al. Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Molecular & cellular proteomics. 2015;14(11):3056-3071. doi: 10.1074/mcp.M115.048850

Author

Colak, Gozde ; Pougovkina, Olga ; Dai, Lunzhi et al. / Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. In: Molecular & cellular proteomics. 2015 ; Vol. 14, No. 11. pp. 3056-3071.

BibTeX

@article{a67906deecd24ee7a5cd0d216194cf4c,
title = "Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation",
abstract = "The protein substrates of sirtuin 5-regulated lysine malonylation (Kmal) remain unknown, hindering its functional analysis. In this study, we carried out proteomic screening, which identified 4042 Kmal sites on 1426 proteins in mouse liver and 4943 Kmal sites on 1822 proteins in human fibroblasts. Increased malonyl-CoA levels in malonyl-CoA decarboxylase (MCD)-deficient cells induces Kmal levels in substrate proteins. We identified 461 Kmal sites showing more than a 2-fold increase in response to MCD deficiency as well as 1452 Kmal sites detected only in MCD-/- fibroblast but not MCD+/+ cells, suggesting a pathogenic role of Kmal in MCD deficiency. Cells with increased lysine malonylation displayed impaired mitochondrial function and fatty acid oxidation, suggesting that lysine malonylation plays a role in pathophysiology of malonic aciduria. Our study establishes an association between Kmal and a genetic disease and offers a rich resource for elucidating the contribution of the Kmal pathway and malonyl-CoA to cellular physiology and human diseases",
author = "Gozde Colak and Olga Pougovkina and Lunzhi Dai and Minjia Tan and {te Brinke}, Heleen and He Huang and Zhongyi Cheng and Jeongsoon Park and Xuelian Wan and Xiaojing Liu and Yue, {Wyatt W.} and Wanders, {Ronald J. A.} and Locasale, {Jason W.} and Lombard, {David B.} and {de Boer}, {Vincent C. J.} and Yingming Zhao",
year = "2015",
doi = "10.1074/mcp.M115.048850",
language = "English",
volume = "14",
pages = "3056--3071",
journal = "Molecular & cellular proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "11",

}

RIS

TY - JOUR

T1 - Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation

AU - Colak, Gozde

AU - Pougovkina, Olga

AU - Dai, Lunzhi

AU - Tan, Minjia

AU - te Brinke, Heleen

AU - Huang, He

AU - Cheng, Zhongyi

AU - Park, Jeongsoon

AU - Wan, Xuelian

AU - Liu, Xiaojing

AU - Yue, Wyatt W.

AU - Wanders, Ronald J. A.

AU - Locasale, Jason W.

AU - Lombard, David B.

AU - de Boer, Vincent C. J.

AU - Zhao, Yingming

PY - 2015

Y1 - 2015

N2 - The protein substrates of sirtuin 5-regulated lysine malonylation (Kmal) remain unknown, hindering its functional analysis. In this study, we carried out proteomic screening, which identified 4042 Kmal sites on 1426 proteins in mouse liver and 4943 Kmal sites on 1822 proteins in human fibroblasts. Increased malonyl-CoA levels in malonyl-CoA decarboxylase (MCD)-deficient cells induces Kmal levels in substrate proteins. We identified 461 Kmal sites showing more than a 2-fold increase in response to MCD deficiency as well as 1452 Kmal sites detected only in MCD-/- fibroblast but not MCD+/+ cells, suggesting a pathogenic role of Kmal in MCD deficiency. Cells with increased lysine malonylation displayed impaired mitochondrial function and fatty acid oxidation, suggesting that lysine malonylation plays a role in pathophysiology of malonic aciduria. Our study establishes an association between Kmal and a genetic disease and offers a rich resource for elucidating the contribution of the Kmal pathway and malonyl-CoA to cellular physiology and human diseases

AB - The protein substrates of sirtuin 5-regulated lysine malonylation (Kmal) remain unknown, hindering its functional analysis. In this study, we carried out proteomic screening, which identified 4042 Kmal sites on 1426 proteins in mouse liver and 4943 Kmal sites on 1822 proteins in human fibroblasts. Increased malonyl-CoA levels in malonyl-CoA decarboxylase (MCD)-deficient cells induces Kmal levels in substrate proteins. We identified 461 Kmal sites showing more than a 2-fold increase in response to MCD deficiency as well as 1452 Kmal sites detected only in MCD-/- fibroblast but not MCD+/+ cells, suggesting a pathogenic role of Kmal in MCD deficiency. Cells with increased lysine malonylation displayed impaired mitochondrial function and fatty acid oxidation, suggesting that lysine malonylation plays a role in pathophysiology of malonic aciduria. Our study establishes an association between Kmal and a genetic disease and offers a rich resource for elucidating the contribution of the Kmal pathway and malonyl-CoA to cellular physiology and human diseases

U2 - 10.1074/mcp.M115.048850

DO - 10.1074/mcp.M115.048850

M3 - Article

C2 - 26320211

VL - 14

SP - 3056

EP - 3071

JO - Molecular & cellular proteomics

JF - Molecular & cellular proteomics

SN - 1535-9476

IS - 11

ER -

ID: 2683671