Abstract:
:p8 is an 80 amino-acid polypeptide identified because of its remarkable over-expression in the stressed pancreas. This protein, apparently devoid of enzymatic activity, is a powerful regulator of several intracellular pathways, suggesting that it has to interact with several molecular partners to modulate their activity. We used two-hybrid screening of a pre-transformed human testes cDNA library to identify some of these partners. One of them was the multifunctional protein Jab1, its interaction with p8 being confirmed by His6-pull down and co-immunoprecipitation assays. In addition, we could show that the two proteins co-localized in the cell. Our functional data demonstrate that Jab1 requires direct interaction with p8 to induce the translocation of p27 from nucleus to cytoplasm and its subsequent degradation. Experiments showing that the knock-down of p8 expression results in a strong inhibition of Jab1 activity confirmed that the mechanism by which Jab1 promotes cell growth by decreasing p27 level is p8-dependent.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Malicet C,Hoffmeister A,Moreno S,Closa D,Dagorn JC,Vasseur S,Iovanna JLdoi
10.1016/j.bbrc.2005.11.018subject
Has Abstractpub_date
2006-01-06 00:00:00pages
284-9issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(05)02530-1journal_volume
339pub_type
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