Fhit modulation of the Akt-survivin pathway in lung cancer cells: Fhit-tyrosine 114 (Y114) is essential
Fhit modulation of the Akt-survivin pathway in lung cancer cells: Fhit-tyrosine 114 (Y114) is essential
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DOI:
10.1038/sj.onc.1209323
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发表时间:
2006-05-01
期刊:
影响因子:
8
通讯作者:
Huebner, K.
中科院分区:
文献类型:
--
作者:
Semba, S.;Trapasso, F.;Huebner, K.
The Fhit tumor suppressor binds and hydrolyses diadenosine polyphosphates and the Fhit - substrate complex has been proposed as a proapoptotic effector, as determined by infection of susceptible cancer cells with adenoviruses carrying wild- type fragile histidine triad ( FHIT) or catalytic site mutants. The highly conserved Fhit tyrosine 114 ( Y114), within the unstructured loop C- terminal of the catalytic site, can be phosphorylated by Src family tyrosine kinases, although endogenous phospho- Fhit is rarely detected. To explore the importance of Y114 and identify Fhit- mediated signaling events, wild- type and Y114 mutant FHIT- expressing adenoviruses were introduced into two human lung cancer cell lines. Caspase-dependent apoptosis was effectively induced only by wildtype but not Y114 mutant Fhit proteins. By expression proling of FHIT versus mutant FHIT- infected cells, we found that survivin, an Inhibitor of Apoptosis Protein ( IAP) family member, was significantly decreased by wildtype Fhit. In addition, Fhit inhibited activity of Akt, a key effector in the phosphatidylinositol 3- OH kinase ( PI3K) pathway; loss of endogenous Fhit expression caused increased Akt activity in vitro and in vivo, and overexpression of constitutively active Akt inhibited Fhit-induced apoptosis. The results indicate that the Fhit Y114 residue plays a critical role in Fhit- induced apoptosis, occurring through inactivation of the PI3K- Akt- survivin signal pathway.