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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2009-5-11
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pubmed:abstractText |
Adipocyte fatty acid-binding protein (AFABP/aP2) facilitates the intracellular solubilization and trafficking of lipids within the aqueous environment of the cell. Studies in the AFABP/aP2 knock-out mouse suggest that the protein may have roles in cellular processes broader than lipid transport. We present herein the finding that AFABP/aP2 interacts with JAK2 in a fatty acid-dependent manner. This interaction was established using yeast two-hybrid analysis, co-immunoprecipitation from adipose tissue, and 3T3-L1 adipocytes as well as in 293 cells overexpressing JAK2 and AFABP/aP2. Mutational analysis of AFABP/aP2 (R126L/Y128F) revealed that fatty acid binding activity is necessary for the interaction and that Asp(18) of the helix-turn-helix motif forms a component of the interaction domain. Mutational analysis of JAK2 (Y1007F/Y1008F) revealed that AFABP/aP2 associates with the basal unphosphorylated form of the protein. Interleukin-6, but not interleukin-10, stimulated phosphorylation of STAT3, and induction of SOCS3 mRNA expression were potentiated in a time- and dose-dependent manner in macrophage cell lines derived from AFABP/aP2-EFABP/mal1 double knock-out mice relative to cells from wild type animals. These results suggest that ligand-bound AFABP/aP2 binds to and attenuates JAK2 signaling and establishes a new role for AFABP/aP2 as a fatty acid sensor affecting cellular metabolism via protein-protein interactions.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-10224167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-10318917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-10851057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-10856918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-11205376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-11385507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-11682468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-12377750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-12454272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-12626585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-12754505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-12754506,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-14744442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-15143187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-15353487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-15456755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-15530433,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-15684432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-16054052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-17412346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-17579051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-17785468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-18174459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-18487233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-18820256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-4079980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-8134389,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-8910278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-9111318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-9202125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-9287210,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-9343427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-9716487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19318353-9849941
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-10,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Jak2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Socs3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Stat3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Suppressor of Cytokine Signaling...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13473-80
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pubmed:dateRevised |
2010-12-3
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pubmed:meshHeading |
pubmed-meshheading:19318353-Animals,
pubmed-meshheading:19318353-Mice,
pubmed-meshheading:19318353-Fatty Acids,
pubmed-meshheading:19318353-Phosphorylation,
pubmed-meshheading:19318353-RNA, Messenger,
pubmed-meshheading:19318353-Biological Transport,
pubmed-meshheading:19318353-Protein Binding,
pubmed-meshheading:19318353-Protein Structure, Tertiary,
pubmed-meshheading:19318353-Gene Expression Regulation,
pubmed-meshheading:19318353-Signal Transduction,
pubmed-meshheading:19318353-Adipocytes,
pubmed-meshheading:19318353-Mutation, Missense,
pubmed-meshheading:19318353-Fatty Acid-Binding Proteins,
pubmed-meshheading:19318353-Interleukin-6
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