Biopolym. Cell. 2013; 29(6):468-472.
http://dx.doi.org/10.7124/bc.00083B
Structure and Function of Biopolymers
Adaptor protein TDRD7 is co-localized with ribosomal protein S6 kinases S6K1 and S6K2 in cell lines of different tissue origin
1Skorokhod O. M., 1Khoruzhenko A. I., 1Filonenko V. V.
  1. State Key Laboratory of Molecular and Cellular Biology
    Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

Our previous studies have shown that S6K1 and S6K2 protein kinases form the complexes with newly identified adaptor protein TDRD7, which is involved in regulation of cytoskeleton dynamics, mRNA transport, protein translation, piRNAs processing and transposons silensing. Aim Determination the subcellular localization of S6K1-TDRD7 and S6K2-TDRD7 protein complexes. Methods. Immunofluorescense microscopy was used to study co-localization of S6K1/S6K2 and TDRD7 in HEK293, HEPG2 cell lines as well as in rat primary hippocampal neurons using primary polyclonal anti-S6K1 antibodies, monoclonal anti-S6K2 and anti- TDRD7 antibodies. Results. It was found that S6K1 is co-localized with TDRD7 in perinuclear region of HEK293 cells. S6K1 and S6K2 were also co-localized with TDRD7 in perinuclear region of HEPG2 cells and in soma of primary rat hippocampal neurons. Conclusions. In this report we provide an additional experimental evidences of possible S6K1-TDRD7 and S6K2-TDRD7 complexes formation in cells of different tissue origins that may reflect their potential physiological importance. However, elucidation of the exact composition of these complexes and their role in cell physiology requires additional studies.
Keywords: S6K1, S6K2, TDRD7, immunocytochemical analysis
Full text: (PDF, in English)

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