Abstract:
:Akt/PKB is a serine/threonine kinase that promotes tumor cell growth by phosphorylating transcription factors and cell cycle proteins. There is particular interest in finding tumor-specific substrates for Akt to understand how this protein functions in cancer and to provide new avenues for therapeutic targeting. Our laboratory sought to identify novel Akt substrates that are expressed in breast cancer. In this study, we determined that activated Akt is positively correlated with the protein expression of the transcription/translation factor Y-box binding protein-1 (YB-1) in primary breast cancer by screening tumor tissue microarrays. We therefore questioned whether Akt and YB-1 might be functionally linked. Herein, we illustrate that activated Akt binds to and phosphorylates the YB-1 cold shock domain at Ser102. We then addressed the functional significance of disrupting Ser102 by mutating it to Ala102. Following the stable expression of Flag:YB-1 and Flag:YB-1 (Ala102) in MCF-7 cells, we observed that disruption of the Akt phosphorylation site on YB-1 suppressed tumor cell growth in soft agar and in monolayer. This correlated with an inhibition of nuclear translocation by the YB-1(Ala102) mutant. In conclusion, YB-1 is a new Akt substrate and disruption of this specific site inhibits tumor cell growth.
journal_name
Oncogenejournal_title
Oncogeneauthors
Sutherland BW,Kucab J,Wu J,Lee C,Cheang MC,Yorida E,Turbin D,Dedhar S,Nelson C,Pollak M,Leighton Grimes H,Miller K,Badve S,Huntsman D,Blake-Gilks C,Chen M,Pallen CJ,Dunn SEdoi
10.1038/sj.onc.1208590subject
Has Abstractpub_date
2005-06-16 00:00:00pages
4281-92issue
26eissn
0950-9232issn
1476-5594pii
1208590journal_volume
24pub_type
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