INVESTIGADORES
MORENO Silvia Margarita
artículos
Título:
Interaction of the stress protein p8 with Jab1 is required for Jab1-dependent p27 nuclear-to-cytoplasm translocation
Autor/es:
MALICET C; HOFFMEISTER A; MORENO S; CLOSA D; DAGORN JC; VASSEUR S; IOVANNA JL
Revista:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Referencias:
Año: 2005 vol. 339 p. 284 - 289
ISSN:
0006-291X
Resumen:
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.
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.
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.
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.
6-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.