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Effects of cytosolic RIP140 in adipocyte glucose uptake
Author(s) -
Lin YiWei,
Ho PingChih,
Gupta Pawan,
Tsui YaoChen,
Ha Sung Gil,
Tsai NienPei,
Wei LiNa
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.215.7
Subject(s) - cytosol , chemistry , cytoplasm , phosphorylation , adipocyte , glucose uptake , protein kinase c , microbiology and biotechnology , insulin , biochemistry , endocrinology , biology , enzyme , adipose tissue
Receptor interacting protein 140 (RIP140) is a versatile transcriptional co‐repressor and plays roles in metabolic processes. Our previous studies showed that protein kinase C epsilon (PKC epsilon) could trigger RIP140 export to the cytoplasm through coordination of phosphorylation and arginine‐methylation. Here, we found that the expression of cytosolic RIP140 decreased basal and insulin‐stimulated glucose uptake in 3T3‐L1 adipocyte. Targeting PKC epsilon by siRNA or specific inhibitor, a trigger inhibiting RIP140 translocation to cytoplasm, also improves glucose uptake. In RIP140 null adipocyte, re‐expression of RIP140 mutant mimicking PKC epsilon stimulated phosphorylation decreased insulin‐stimulated glucose uptake. Re‐expressing RIP140 mutant deficient in PKC epsilon stimulated phosphorylation had no effects on insulin‐stimulated glucose uptake. These results indicate nuclear PKC epsilon activation promotes RIP140 export from nucleus to cytoplasm, and the cytosolic RIP140 exerts a novel activity in the cytoplasm to regulate glucose uptake and insulin sensitivity in adipocyte. This work was supported by DA11190, DA11806, DK54733, DK60521, K02‐DA13926 to L.‐N. W.