Acyl-CoA metabolism and partitioning

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Acyl-CoA metabolism and partitioning. / Grevengoed, Trisha J; Klett, Eric L; Coleman, Rosalind A.

In: Annual Review of Nutrition, Vol. 34, 2014, p. 1-30.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Grevengoed, TJ, Klett, EL & Coleman, RA 2014, 'Acyl-CoA metabolism and partitioning', Annual Review of Nutrition, vol. 34, pp. 1-30. https://doi.org/10.1146/annurev-nutr-071813-105541

APA

Grevengoed, T. J., Klett, E. L., & Coleman, R. A. (2014). Acyl-CoA metabolism and partitioning. Annual Review of Nutrition, 34, 1-30. https://doi.org/10.1146/annurev-nutr-071813-105541

Vancouver

Grevengoed TJ, Klett EL, Coleman RA. Acyl-CoA metabolism and partitioning. Annual Review of Nutrition. 2014;34:1-30. https://doi.org/10.1146/annurev-nutr-071813-105541

Author

Grevengoed, Trisha J ; Klett, Eric L ; Coleman, Rosalind A. / Acyl-CoA metabolism and partitioning. In: Annual Review of Nutrition. 2014 ; Vol. 34. pp. 1-30.

Bibtex

@article{2190f861a27f4924bfe174b68fa1ce07,
title = "Acyl-CoA metabolism and partitioning",
abstract = "Long-chain fatty acyl-coenzyme As (CoAs) are critical regulatory molecules and metabolic intermediates. The initial step in their synthesis is the activation of fatty acids by one of 13 long-chain acyl-CoA synthetase isoforms. These isoforms are regulated independently and have different tissue expression patterns and subcellular locations. Their acyl-CoA products regulate metabolic enzymes and signaling pathways, become oxidized to provide cellular energy, and are incorporated into acylated proteins and complex lipids such as triacylglycerol, phospholipids, and cholesterol esters. Their differing metabolic fates are determined by a network of proteins that channel the acyl-CoAs toward or away from specific metabolic pathways and serve as the basis for partitioning. This review evaluates the evidence for acyl-CoA partitioning by reviewing experimental data on proteins that are believed to contribute to acyl-CoA channeling, the metabolic consequences of loss of these proteins, and the potential role of maladaptive acyl-CoA partitioning in the pathogenesis of metabolic disease and carcinogenesis.",
keywords = "Acyl Coenzyme A, Animals, Cell Membrane, Coenzyme A Ligases, Endoplasmic Reticulum, Fatty Acid Transport Proteins, Gene Expression Regulation, Humans, Lipid Metabolism, Models, Biological, Protein Isoforms, Protein Transport",
author = "Grevengoed, {Trisha J} and Klett, {Eric L} and Coleman, {Rosalind A}",
year = "2014",
doi = "10.1146/annurev-nutr-071813-105541",
language = "English",
volume = "34",
pages = "1--30",
journal = "Annual Review of Nutrition",
issn = "0199-9885",
publisher = "Annual Reviews, inc.",

}

RIS

TY - JOUR

T1 - Acyl-CoA metabolism and partitioning

AU - Grevengoed, Trisha J

AU - Klett, Eric L

AU - Coleman, Rosalind A

PY - 2014

Y1 - 2014

N2 - Long-chain fatty acyl-coenzyme As (CoAs) are critical regulatory molecules and metabolic intermediates. The initial step in their synthesis is the activation of fatty acids by one of 13 long-chain acyl-CoA synthetase isoforms. These isoforms are regulated independently and have different tissue expression patterns and subcellular locations. Their acyl-CoA products regulate metabolic enzymes and signaling pathways, become oxidized to provide cellular energy, and are incorporated into acylated proteins and complex lipids such as triacylglycerol, phospholipids, and cholesterol esters. Their differing metabolic fates are determined by a network of proteins that channel the acyl-CoAs toward or away from specific metabolic pathways and serve as the basis for partitioning. This review evaluates the evidence for acyl-CoA partitioning by reviewing experimental data on proteins that are believed to contribute to acyl-CoA channeling, the metabolic consequences of loss of these proteins, and the potential role of maladaptive acyl-CoA partitioning in the pathogenesis of metabolic disease and carcinogenesis.

AB - Long-chain fatty acyl-coenzyme As (CoAs) are critical regulatory molecules and metabolic intermediates. The initial step in their synthesis is the activation of fatty acids by one of 13 long-chain acyl-CoA synthetase isoforms. These isoforms are regulated independently and have different tissue expression patterns and subcellular locations. Their acyl-CoA products regulate metabolic enzymes and signaling pathways, become oxidized to provide cellular energy, and are incorporated into acylated proteins and complex lipids such as triacylglycerol, phospholipids, and cholesterol esters. Their differing metabolic fates are determined by a network of proteins that channel the acyl-CoAs toward or away from specific metabolic pathways and serve as the basis for partitioning. This review evaluates the evidence for acyl-CoA partitioning by reviewing experimental data on proteins that are believed to contribute to acyl-CoA channeling, the metabolic consequences of loss of these proteins, and the potential role of maladaptive acyl-CoA partitioning in the pathogenesis of metabolic disease and carcinogenesis.

KW - Acyl Coenzyme A

KW - Animals

KW - Cell Membrane

KW - Coenzyme A Ligases

KW - Endoplasmic Reticulum

KW - Fatty Acid Transport Proteins

KW - Gene Expression Regulation

KW - Humans

KW - Lipid Metabolism

KW - Models, Biological

KW - Protein Isoforms

KW - Protein Transport

U2 - 10.1146/annurev-nutr-071813-105541

DO - 10.1146/annurev-nutr-071813-105541

M3 - Journal article

C2 - 24819326

VL - 34

SP - 1

EP - 30

JO - Annual Review of Nutrition

JF - Annual Review of Nutrition

SN - 0199-9885

ER -

ID: 146698774