Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
ISSN: 0974-276X
Jennifer L. Frahm
Tanzania
Research Article
Phosphorylation and Acetylation of Acyl-Coa Synthetase- I
Author(s): Jennifer L. Frahm, Lei O. Li, Trisha J. Grevengoed and Rosalind A. ColemanJennifer L. Frahm, Lei O. Li, Trisha J. Grevengoed and Rosalind A. Coleman
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 acetylate.. View More»
DOI:
10.4172/jpb.1000180