TY - JOUR
T1 - Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation
AU - Black, Paul N.
AU - DiRusso, Concetta C.
N1 - Funding Information:
The material reviewed in this article is the result of work from many laboratories and individuals. We apologize if we have missed some of the vast literature on yeast acyl-CoA synthetases accrued over the years. We especially thank members of the Black and DiRusso FATTT lab for their hard work, insight and stimulating criticisms. The research in our laboratory as reviewed here has been generously supported by the National Institutes of Health, the American Heart Association, the National Science Foundation and the Charitable Leadership Foundation.
PY - 2007/3
Y1 - 2007/3
N2 - Acyl-CoA synthetases (ACSs) are a family of enzymes that catalyze the thioesterification of fatty acids with coenzymeA to form activated intermediates, which play a fundamental role in lipid metabolism and homeostasis of lipid-related processes. The products of the ACS enzyme reaction, acyl-CoAs, are required for complex lipid synthesis, energy production via β-oxidation, protein acylation and fatty-acid dependent transcriptional regulation. ACS enzymes are also necessary for fatty acid import into cells by the process of vectorial acylation. The yeast Saccharomyces cerevisiae has four long chain ACS enzymes designated Faa1p through Faa4p, one very long chain ACS named Fat1p and one ACS, Fat2p, for which substrate specificity has not been defined. Pivotal roles have been defined for Faa1p and Faa4p in fatty acid import, β-oxidation and transcriptional control mediated by the transcription factors Oaf1p/Pip2p and Mga2p/Spt23p. Fat1p is a bifunctional protein required for fatty acid transport of long chain fatty acids, as well as activation of very long chain fatty acids. This review focuses on the various roles yeast ACS enzymes play in cellular metabolism targeting especially the functions of specific isoforms in fatty acid transport, metabolism and energy production. We will also present evidence from directed experimentation, as well as information obtained by mining the molecular biological databases suggesting the long chain ACS enzymes are required in protein acylation, vesicular trafficking, signal transduction pathways and cell wall synthesis.
AB - Acyl-CoA synthetases (ACSs) are a family of enzymes that catalyze the thioesterification of fatty acids with coenzymeA to form activated intermediates, which play a fundamental role in lipid metabolism and homeostasis of lipid-related processes. The products of the ACS enzyme reaction, acyl-CoAs, are required for complex lipid synthesis, energy production via β-oxidation, protein acylation and fatty-acid dependent transcriptional regulation. ACS enzymes are also necessary for fatty acid import into cells by the process of vectorial acylation. The yeast Saccharomyces cerevisiae has four long chain ACS enzymes designated Faa1p through Faa4p, one very long chain ACS named Fat1p and one ACS, Fat2p, for which substrate specificity has not been defined. Pivotal roles have been defined for Faa1p and Faa4p in fatty acid import, β-oxidation and transcriptional control mediated by the transcription factors Oaf1p/Pip2p and Mga2p/Spt23p. Fat1p is a bifunctional protein required for fatty acid transport of long chain fatty acids, as well as activation of very long chain fatty acids. This review focuses on the various roles yeast ACS enzymes play in cellular metabolism targeting especially the functions of specific isoforms in fatty acid transport, metabolism and energy production. We will also present evidence from directed experimentation, as well as information obtained by mining the molecular biological databases suggesting the long chain ACS enzymes are required in protein acylation, vesicular trafficking, signal transduction pathways and cell wall synthesis.
KW - Acyl-CoA
KW - Acyl-CoA synthetase
KW - Fatty acid transport
KW - Lipogenesis
KW - Protein acylation
KW - Vectorial acylation
KW - Yeast
KW - β-oxidation
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U2 - 10.1016/j.bbalip.2006.05.003
DO - 10.1016/j.bbalip.2006.05.003
M3 - Review article
C2 - 16798075
AN - SCOPUS:33947316606
VL - 1771
SP - 286
EP - 298
JO - BBA - Specialised Section On Lipids and Related Subjects
JF - BBA - Specialised Section On Lipids and Related Subjects
SN - 1388-1981
IS - 3
ER -