Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 290: C1477-C1486, 2006. First published December 28, 2005; doi:10.1152/ajpcell.00374.2005
0363-6143/06 $8.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
290/6/C1477    most recent
00374.2005v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via ISI Web of Science (4)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lu, M.
Right arrow Articles by Shyy, J. Y.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lu, M.
Right arrow Articles by Shyy, J. Y.-J.

CELLULAR METABOLISM

Sterol regulatory element-binding protein 1 is negatively modulated by PKA phosphorylation

Min Lu and John Y.-J. Shyy

Division of Biomedical Sciences, University of California, Riverside, Riverside, California

Submitted 22 July 2005 ; accepted in final form 21 December 2005

Sterol regulatory element-binding protein (SREBP)-1a and -1c are key transcription factors that regulate lipid biosynthesis in cells. We identified that Ser338 located at the NH2 terminus of SREBP-1a is a PKA phosphorylation site in vitro and in HepG2 cells. PKA phosphorylation of this site attenuated DNA occupancy, as revealed by chromatin immunoprecipitation assay, and the ensuing transactivation. In contrast, replacing Ser with Ala [SREBP-1a(N)-S338A] increased transactivation. Although it forms heterodimers with the wild-type SREBP-1a(N) or S338A but not a homodimer with itself, SREBP-1a(N)-S338D (replacing Ser with Asp) decreased DNA binding. Ser314 of SREBP-1c, the counterpart of SREBP-1a Ser338, was also phosphorylated by PKA. Accordingly, the adenovirus-mediated expression of SREBP-1c(N)-S314D in HepG2 cells retarded lipogenesis. Our results indicate that the cAMP-PKA pathway, by phosphorylating SREBP-1, may modulate lipid metabolism in liver cell lines.

metabolism; glucagon; insulin; lipogenesis


Address for reprint requests and other correspondence: J. Y.-J. Shyy, Division of Biomedical Sciences, Univ. of California, Riverside, Riverside, CA 92521-0121 (e-mail: john.shyy{at}ucr.edu)




This article has been cited by other articles:


Home page
 J. Gen. Virol.Home page
J.-K. Oem, C. Jackel-Cram, Y.-P. Li, Y. Zhou, J. Zhong, H. Shimano, L. A. Babiuk, and Q. Liu
Activation of sterol regulatory element-binding protein 1c and fatty acid synthase transcription by hepatitis C virus non-structural protein 2
J. Gen. Virol., May 1, 2008; 89(5): 1225 - 1230.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2006 by the American Physiological Society.