Document Detail


Ypk1, the yeast orthologue of the human serum- and glucocorticoid-induced kinase, is required for efficient uptake of fatty acids.
MedLine Citation:
PMID:  20516150     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Fatty acids constitute an important energy source for various tissues. The mechanisms that mediate and control uptake of free fatty acids from the circulation, however, are poorly understood. Here we show that efficient fatty-acid uptake by yeast cells requires the protein kinase Ypk1, the orthologue of the human serum- and glucocorticoid-induced kinase Sgk1. ypk1Delta mutant cells fail to grow under conditions that render cells auxotrophic for fatty acids, show a reduced uptake of radiolabelled or fluorescently labelled fatty acids, lack the facilitated component of the uptake activity, and have elevated levels of fatty acids in a bovine serum albumin (BSA) back-extractable compartment. Efficient fatty-acid uptake and/or incorporation requires the protein-kinase activity of Ypk1, because a kinase-dead point-mutant allele of YPK1 is defective in this process. This function of Ypk1 in fatty-acid uptake and/or incorporation is functionally conserved, because expression of the human Sgk1 kinase rescues ypk1Delta mutant yeast. These observations suggest that Ypk1 and possibly the human Sgk1 kinase affect fatty-acid uptake and thus energy homeostasis through regulating endocytosis. Consistent with such a proposition, mutations that block early steps of endocytosis display reduced levels of fatty-acid uptake.
Authors:
Nicolas Jacquier; Roger Schneiter
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-06-01
Journal Detail:
Title:  Journal of cell science     Volume:  123     ISSN:  1477-9137     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-06-17     Completed Date:  2010-10-18     Revised Date:  2011-11-02    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  2218-27     Citation Subset:  IM    
Affiliation:
Department of Medicine, Division of Biochemistry, University of Fribourg, Chemin du Musee 5, 1700 Fribourg, Switzerland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Biological Transport
Cattle
Cell Membrane / metabolism
Endocytosis / physiology*
Fatty Acids / metabolism*
Glycogen Synthase Kinase 3 / genetics,  metabolism*
Humans
Immediate-Early Proteins / genetics,  metabolism
Mutation
Protein-Serine-Threonine Kinases / genetics,  metabolism
Saccharomyces cerevisiae / cytology,  physiology
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Serum Albumin, Bovine / chemistry,  metabolism
Chemical
Reg. No./Substance:
0/Fatty Acids; 0/Immediate-Early Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Serum Albumin, Bovine; EC 2.7.11.1/MCK1 protein, S cerevisiae; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/serum-glucocorticoid regulated kinase; EC 2.7.11.26/Glycogen Synthase Kinase 3

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Bat3 promotes the membrane integration of tail-anchored proteins.
Next Document:  Plk4 trans-autophosphorylation regulates centriole number by controlling {beta}TrCP-mediated degrada...