http://www.cnr.it/ontology/cnr/individuo/prodotto/ID20861
Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer. (Articolo in rivista)
- Type
- Label
- Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer. (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Alternative label
Viglietto G. 1, Motti M.L. 1, Bruni P. 2, Melillo R.M. 1, D'Alessio A. 3, Califano D. 3, Vinci F. 4, Chiappetta G. 3, Tsichlis P. 5, Bellacosa A. 6-7, Fusco A. 1, Santoro M. 1 (2002)
Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer.
in Nature medicine (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Viglietto G. 1, Motti M.L. 1, Bruni P. 2, Melillo R.M. 1, D'Alessio A. 3, Califano D. 3, Vinci F. 4, Chiappetta G. 3, Tsichlis P. 5, Bellacosa A. 6-7, Fusco A. 1, Santoro M. 1 (literal)
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- Impact Factor = 27,906;
Interdisciplinarietà del prodotto :The Authors belong to different scientific areas, sectors and Istitutions. The paper was in collaboration with International Institutions. (literal)
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- Rivista
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- The cyclin-dependent kinase inhibitor p27(kip1) is a putative tumor suppressor for human cancer. The mechanism underlying p27(kip1) deregulation in human cancer is, however, poorly understood. We demonstrate that the serine/threonine kinase Akt regulates cell proliferation in breast cancer cells by preventing p27(kip1)-mediated growth arrest. Threonine 157 (T157), which maps within the nuclear localization signal of p27(kip1), is a predicted Akt-phosphorylation site. Akt-induced T157 phosphorylation causes retention of p27(kip1) in the cytoplasm, precluding p27(kip1)-induced G1 arrest. Conversely, the p27(kip1)-T157A mutant accumulates in cell nuclei and Akt does not affect p27(kip1)-T157A-mediated cell cycle arrest. Lastly, T157-phosphorylated p27(kip1) accumulates in the cytoplasm of primary human breast cancer cells coincident with Akt activation. Thus, cytoplasmic relocalization of p27(kip1), secondary to Akt-mediated phosphorylation, is a novel mechanism whereby the growth inhibitory properties of p27(kip1) are functionally inactivated and the proliferation of breast cancer cells is sustained. (literal)
- Note
- ISI Web of Science (WOS) (literal)
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- 1 Istituto di Endocrinologia ed Oncologia Sperimentale, CNR c/o Dipartimento di Biologia e Patologia Cellulare e Molecolare, Naples, Italy
2 Dipartimento di Biochimica e Biotecnologie Mediche, Naples, Italy
3 INT \"Fondazione Pascale\", Naples, Italy
4 Dip. Chimica Organica e Biochimica, Naples, Italy
5 Kimmel Cancer Center, Jefferson Medical College, Philadelphia, USA
6 Fox Chase Cancer Center, Philadelphia, USA
7 Dpt. Medical Genetics, Catholic University, Medical School, Rome, Italy (literal)
- Titolo
- Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer. (literal)
- Abstract
- The cyclin-dependent kinase inhibitor p27(kip1) is a putative tumor suppressor for human cancer. The mechanism underlying p27(kip1) deregulation in human cancer is, however, poorly understood. We demonstrate that the serine/threonine kinase Akt regulates cell proliferation in breast cancer cells by preventing p27(kip1)-mediated growth arrest. Threonine 157 (T157), which maps within the nuclear localization signal of p27(kip1), is a predicted Akt-phosphorylation site. Akt-induced T157 phosphorylation causes retention of p27(kip1) in the cytoplasm, precluding p27(kip1)-induced G1 arrest. Conversely, the p27(kip1)-T157A mutant accumulates in cell nuclei and Akt does not affect p27(kip1)-T157A-mediated cell cycle arrest. Lastly, T157-phosphorylated p27(kip1) accumulates in the cytoplasm of primary human breast cancer cells coincident with Akt activation. Thus, cytoplasmic relocalization of p27(kip1), secondary to Akt-mediated phosphorylation, is a novel mechanism whereby the growth inhibitory properties of p27(kip1) are functionally inactivated and the proliferation of breast cancer cells is sustained. (literal)
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