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...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
O. Skorokhod [verfasserIn] G. Panasyuk [verfasserIn] I. Nemazanyy [verfasserIn] I. Gout [verfasserIn] V. Filonenko [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2013 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
In: The Ukrainian Biochemical Journal ; 85(2013), 6, Seite 46-52 volume:85 ; year:2013 ; number:6 ; pages:46-52 |
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| Links: |
Link aufrufen |
|---|
| DOI / URN: |
10.15407/ubj85.06.046 |
|---|
| Katalog-ID: |
DOAJ098368958 |
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| 520 | |a 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. | ||
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Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
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Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
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O. Skorokhod |
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The Ukrainian Biochemical Journal |
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The Ukrainian Biochemical Journal |
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O. Skorokhod G. Panasyuk I. Nemazanyy I. Gout V. Filonenko |
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O. Skorokhod |
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10.15407/ubj85.06.046 |
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verfasserin |
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identification of tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein s6 kinases – s6k1 and s6k2 |
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QD415-436 |
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Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
| abstract |
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. |
| abstractGer |
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. |
| abstract_unstemmed |
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. |
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Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2 |
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https://doi.org/10.15407/ubj85.06.046 https://doaj.org/article/7c4a7cca76c94462b4c7cd63df5a1b63 http://ukrbiochemjournal.org/wp-content/uploads/2015/11/Skorokhod_6_13.pdf https://doaj.org/toc/2409-4943 https://doaj.org/toc/2413-5003 |
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