Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2
Ribosomal protein S6 kinases (S6Ks) are principal regulators of cell size, growth and metabolism. Signaling via the PI3K/mTOR pathway mediates the activation of S6Ks in response to various mitogenic stimuli, nutrients and stresses. To date, the regulation and cellular functions of S6Ks are not fully...
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| Format: | Article |
| Language: | English |
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National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry
2013-12-01
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| Series: | The Ukrainian Biochemical Journal |
| Subjects: | |
| Online Access: | http://ukrbiochemjournal.org/wp-content/uploads/2015/11/Skorokhod_6_13.pdf |
| _version_ | 1797641825557676032 |
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| author | O. Skorokhod G. Panasyuk I. Nemazanyy I. Gout V. Filonenko |
| author_facet | O. Skorokhod G. Panasyuk I. Nemazanyy I. Gout V. Filonenko |
| author_sort | O. Skorokhod |
| collection | DOAJ |
| description | Ribosomal protein S6 kinases (S6Ks) are principal regulators of cell size, growth and metabolism. Signaling via the PI3K/mTOR pathway mediates the activation of S6Ks in response to various mitogenic stimuli, nutrients and stresses. To date, the regulation and cellular functions of S6Ks are not fully understood. Our aim was to investigate and characterize the interaction of S6Ks with the novel binding partner of S6Ks, Tudor domain containing 7 protein (TDRD7), which is a scaffold protein detected in complexes involved in the regulation of cytoskeleton dynamics, mRNA transport and translation, non-coding piRNAs processing and transposons silencing. This interaction was initially detected in the yeast two-hybrid screening of HeLa cDNA library and further confirmed by pull-down and co-immunoprecipitation assays. In addition we demonstrated that TDRD7 can form a complex with other isoform of S6K – S6K2. Notably, both isoforms of S6K were found to phosphorylate TDRD7 in vitro at multiple phosphorylation sites. Altogether, these findings demonstrate that TDRD7 is a novel substrate of S6Ks, suggesting the involvement of S6K signaling in the regulation of TDRD7 cellular functions. |
| first_indexed | 2024-03-11T13:51:17Z |
| format | Article |
| id | doaj.art-7c4a7cca76c94462b4c7cd63df5a1b63 |
| institution | Directory Open Access Journal |
| issn | 2409-4943 2413-5003 |
| language | English |
| last_indexed | 2024-03-11T13:51:17Z |
| publishDate | 2013-12-01 |
| publisher | National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry |
| record_format | Article |
| series | The Ukrainian Biochemical Journal |
| spelling | doaj.art-7c4a7cca76c94462b4c7cd63df5a1b632023-11-02T09:03:57ZengNational Academy of Sciences of Ukraine, Palladin Institute of BiochemistryThe Ukrainian Biochemical Journal2409-49432413-50032013-12-01856465210.15407/ubj85.06.046Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2O. Skorokhod0 G. Panasyuk1I. Nemazanyy2I. Gout3V. Filonenko4Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv;The State Key Laboratory of Molecular and Cellular Biology, Kyiv, Ukraine Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv;Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv;Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv; University College London, United KingdomInstitute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, KyivThe State Key Laboratory of Molecular and Cellular Biology, Kyiv, Ukraine; Ribosomal protein S6 kinases (S6Ks) are principal regulators of cell size, growth and metabolism. Signaling via the PI3K/mTOR pathway mediates the activation of S6Ks in response to various mitogenic stimuli, nutrients and stresses. To date, the regulation and cellular functions of S6Ks are not fully understood. Our aim was to investigate and characterize the interaction of S6Ks with the novel binding partner of S6Ks, Tudor domain containing 7 protein (TDRD7), which is a scaffold protein detected in complexes involved in the regulation of cytoskeleton dynamics, mRNA transport and translation, non-coding piRNAs processing and transposons silencing. This interaction was initially detected in the yeast two-hybrid screening of HeLa cDNA library and further confirmed by pull-down and co-immunoprecipitation assays. In addition we demonstrated that TDRD7 can form a complex with other isoform of S6K – S6K2. Notably, both isoforms of S6K were found to phosphorylate TDRD7 in vitro at multiple phosphorylation sites. Altogether, these findings demonstrate that TDRD7 is a novel substrate of S6Ks, suggesting the involvement of S6K signaling in the regulation of TDRD7 cellular functions.http://ukrbiochemjournal.org/wp-content/uploads/2015/11/Skorokhod_6_13.pdfphosphorylationS6K1S6K2TDRD7 |
| spellingShingle | O. Skorokhod G. Panasyuk I. Nemazanyy I. Gout V. Filonenko Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 The Ukrainian Biochemical Journal phosphorylation S6K1 S6K2 TDRD7 |
| title | Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
| title_full | Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
| title_fullStr | Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
| title_full_unstemmed | Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
| title_short | Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
| title_sort | identification of tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein s6 kinases s6k1 and s6k2 |
| topic | phosphorylation S6K1 S6K2 TDRD7 |
| url | http://ukrbiochemjournal.org/wp-content/uploads/2015/11/Skorokhod_6_13.pdf |
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