alexa Phosphorylation and Acetylation of Acyl-Coa Synthetase-
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Phosphorylation and Acetylation of Acyl-Coa Synthetase- I

Jennifer L. Frahm1,2, Lei O. Li1, Trisha J. Grevengoed and Rosalind A. Coleman*

Department of Nutrition, University of North Carolina, Chapel Hill, North Carolina 27599

1These authors contributed equally to this work

2Current address: Thermo Fisher Scientific, 1400 Northpoint Pkwy, Suite 10, West Palm Beach, FL33407

*Corresponding Author:
Dr. Rosalind A. Coleman
Department of Nutrition
CB 7461, University of North Carolina
Tel: 919-966-7213
Fax: 919-843-8555
E-mail: [email protected]

Received Date: May 24, 2011; Accepted Date: July 20, 2011; Published Date: July 22, 2011

Citation: Frahm JL, Li LO, Grevengoed TJ, Coleman RA (2011) Phosphorylation and Acetylation of Acyl-Coa Synthetase- I. J Proteomics Bioinform 4:129-137. doi:10.4172/jpb.1000180

Copyright: © 2011 Frahm JL, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

Long chain acyl-CoA synthetase 1 (ACSL1) contributes 50 to 90% of total ACSL activity in liver, adipose tissue, and heart and appears to direct the use of long chain fatty acids for energy. Although the functional importance of ACSL1 is becoming clear, little is understood about its post-translational regulation. In order to investigate the post-translational modifications of ACSL1 under different physiological conditions, we overexpressed ACSL1 in hepatocytes, brown adipocytes, and 3T3-L1 differentiated adipocytes, treated these cells with different hormones, and analyzed the resulting phosphorylated and acetylated amino acids by mass spectrometry. We then compared these results to the post-translational modifications observed in vivo in liver and brown adipose tissue after mice were fasted or exposed to a cold environment. We identified universal N-terminal acetylation, 15 acetylated lysines, and 25 phosphorylation sites on ACSL1. Several unique acetylation and phosphorylation sites occurred under conditions in which fatty acid ?-oxidation is normally enhanced. Thirteen of the acetylated lysines had not previously been identified, and none of the phosphorylation sites had been previously identified. Site-directed mutagenesis was used to introduce mutations at three potential acetylation and phosphorylation sites believed to be important for ACSL1 function. At the ATP/AMP binding site and at a highly conserved site near the C terminus, modifications of Ser278 or Lys676, respectively, totally inhibited ACSL1 activity. In contrast, mutations of Lys285 that mimicked acetylation (Lys285Ala and Lys285Gln) reduced ACSL activity, whereas full activity was retained by Lys285Arg, suggesting that acetylation of Lys285 would be likely to decrease ACSL1 activity. These results indicate that ACSL1 is highly modified post-translationally. Several of these modifications would be expected to alter enzymatic function, but others may affect protein stability or protein-protein interactions.

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