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Insulin receptor substrate‐1 (IRS‐1) forms a ribonucleoprotein complex associated with polysomes
Author(s) -
Ozoe Atsufumi,
Sone Meri,
Fukushima Toshiaki,
Kataoka Naoyuki,
Arai Toshiya,
Chida Kazuhiro,
Asano Tomoichiro,
Hakuno Fumihiko,
Takahashi Shin-Ichiro
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.05.066
Subject(s) - ribonucleoprotein , polysome , insulin receptor substrate , insulin receptor , chemistry , substrate (aquarium) , receptor , microbiology and biotechnology , biophysics , insulin , biochemistry , biology , endocrinology , rna , ribosome , insulin resistance , gene , ecology
Insulin receptor substrates (IRSs) are known to play important roles in mediating intracellular insulin‐like growth factors (IGFs)/insulin signaling. In this study, we identified components of messenger ribonucleoprotein (mRNP) as IRS‐1‐associated proteins. IRS‐1 complex formation analysis revealed that IRS‐1 is incorporated into the complexes of molecular mass more than 1000 kDa, which were disrupted by treatment with RNase. Furthermore, oligo(dT) beads precipitated IRS‐1 from cell lysates, showing that the IRS‐1 complexes contained messenger RNA. Taken together with the data that IRS‐1 was fractionated into the polysome‐containing high‐density fractions, we concluded that IRS‐1 forms the novel complexes with mRNPs.