Format

Send to

Choose Destination
Chem Biol. 2015 Mar 19;22(3):412-25. doi: 10.1016/j.chembiol.2015.02.007.

Quantitative analysis of proteome and lipidome dynamics reveals functional regulation of global lipid metabolism.

Author information

1
Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, 5230 Odense, Denmark.
2
Département de Biochimie, Université de Montréal, Succ. Centre-Ville, 6128 Montreal, Quebec H3C 3J7, Canada.
3
Austrian Centre of Industrial Biotechnology, 1190 Vienna, Austria; Department of Biotechnology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
4
Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, 5230 Odense, Denmark. Electronic address: cse@bmb.sdu.dk.

Abstract

Elucidating how and to what extent lipid metabolism is remodeled under changing conditions is essential for understanding cellular physiology. Here, we analyzed proteome and lipidome dynamics to investigate how regulation of lipid metabolism at the global scale supports remodeling of cellular architecture and processes during physiological adaptations in yeast. Our results reveal that activation of cardiolipin synthesis and remodeling supports mitochondrial biogenesis in the transition from fermentative to respiratory metabolism, that down-regulation of de novo sterol synthesis machinery prompts differential turnover of lipid droplet-associated triacylglycerols and sterol esters during respiratory growth, that sphingolipid metabolism is regulated in a previously unrecognized growth stage-specific manner, and that endogenous synthesis of unsaturated fatty acids constitutes an in vivo upstream activator of peroxisomal biogenesis, via the heterodimeric Oaf1/Pip2 transcription factor. Our work demonstrates the pivotal role of lipid metabolism in adaptive processes and provides a resource to investigate its regulation at the cellular level.

PMID:
25794437
DOI:
10.1016/j.chembiol.2015.02.007
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center