The beta subunit of casein kinase 2 as a novel binding partner of the ribosomal protein S6 kinase 1

Adaptor protein TDRD7 is co-localized with ribosomal protein S6 kinases S6K1 and S6K2 in cell lines of different tissue origin

“…Taking into consideration our previous results [10,11] the obtained data also support the idea of possible physiological importance of these complexes formation. However, determination of the exact composition of complexes and elucidation of their role in cells require additional studies.…”

“…Previously, in the course of yeast-two hybrid screening of HeLa cDNA library by S6K1 as a bite we have identified a novel S6K1/2 binding partner -Tudor domain containing 7 protein (TDRD7) [10]. Further studies confirmed the formation of S6K1/TDRD7 and S6K2/ TDRD7 complexes in vivo [11].…”

Identification of Tudor domain containing 7 protein as a novel partner and a substrate for ribosomal protein S6 kinaseS – S6K1 and S6K2

“…The yeast twohybrid screen of a HeLa cDNA library with S6K1 as a bait allowed us to identify a number of known and novel binding partners [34]. Among them, 17 cDNA clones contained fulllength coding sequence for TDRD7 protein.…”

PI3K/mTOR/S6K signaling pathway – new players and new functional links

“…According to the functional studies using cell's models the CK2-mediated S6K1 phosphorylation affects its nucleocytoplasmic shuttling and en-hancers nuclear export. We also provided evidence that nuclear export of S6K1 is mediated by a CRM1-dependent mechanism [31][32][33].…”

“…To identify novel functional links of S6Ks we have employed the yeast two-hybrid system to search for novel S6K binding partners and used a full length S6K1 as «bait» [29][30][31]. One of the protein partner identified was regulatory b subunit of protein kinase 2 (CK2).…”