c-FLIPL enhances anti-apoptotic Akt functions by modulation of Gsk3β activity View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2010-12

AUTHORS

C Quintavalle, M Incoronato, L Puca, M Acunzo, C Zanca, G Romano, M Garofalo, M Iaboni, C M Croce, G Condorelli

ABSTRACT

Akt is a serine-threonine kinase that has an important role in transducing survival signals. Akt also regulates a number of proteins involved in the apoptotic process. To find new Akt interactors, we performed a two-hybrid screening in yeast using full-length Akt cDNA as bait and a human cDNA heart library as prey. Among 200 clones obtained, two of them were identified as coding for the c-FLIP(L) protein. c-FLIP(L) is an endogenous inhibitor of death receptor-induced apoptosis through the caspase-8 pathway. Using co-immunoprecipitation experiments of either transfected or endogenous proteins, we confirmed the interaction between Akt and c-FLIP(L). Furthermore, we observed that c-FLIP(L) overexpression interferes with Gsk3-β phosphorylation levels. Moreover, through its effects on Gsk3β, c-FLIP(L) overexpression in cancer cells induced resistance to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL). This effect was mediated by the regulation of p27(Kip1) and caspase-3 expression. These results indicate the existence of a new mechanism of resistance to TRAIL in cancer cells, and unexpected functions of c-FLIP(L). More... »

PAGES

1908

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/cdd.2010.65

DOI

http://dx.doi.org/10.1038/cdd.2010.65

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048340244

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20508645


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