Chiuso, Francesco (2017) Regulation of PTP1B stability and signaling by the PKA scaffold protein praja2. [Tesi di dottorato]
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Phd_Thesis_Francesco_Chiuso_XXX_ciclo.pdf Download (2MB) | Anteprima |
| Tipologia del documento: | Tesi di dottorato |
|---|---|
| Lingua: | English |
| Titolo: | Regulation of PTP1B stability and signaling by the PKA scaffold protein praja2 |
| Autori: | Autore Email Chiuso, Francesco francesco.chiuso@gmail.com |
| Data: | 10 Dicembre 2017 |
| Numero di pagine: | 57 |
| Istituzione: | Università degli Studi di Napoli Federico II |
| Dipartimento: | dep14 |
| Dottorato: | phd054 |
| Ciclo di dottorato: | 30 |
| Coordinatore del Corso di dottorato: | nome email Avvedimento, Vittorio Enrico vittorioenrico.avvedimento@unina.it |
| Tutor: | nome email Feliciello, Antonio [non definito] |
| Data: | 10 Dicembre 2017 |
| Numero di pagine: | 57 |
| Parole chiave: | praja2 PTP1B PKA cAMP UPS |
| Settori scientifico-disciplinari del MIUR: | Area 06 - Scienze mediche > MED/04 - Patologia generale |
| Depositato il: | 27 Dic 2017 17:16 |
| Ultima modifica: | 22 Mar 2019 11:09 |
| URI: | http://www.fedoa.unina.it/id/eprint/12144 |
Abstract
Protein tyrosine phosphatase 1B (PTP1B) is a non-transmembrane protein implicated as negative regulator in the insulin and leptin pathways. PTP1B is also implicated in the development of breast cancer due to its dephosphorylating role on the proto-oncogene Src. During these years, PTP1B has emerged as a promising potential therapeutic target for the treatment of the type 2 diabetes. PTP1B control mechanisms are still controversial and not well understood. Here, I've contributed to identify a novel mechanism of regulation of PTP1B mediated by the ubiquitin-proteasome pathway. We identify the E3 ligase praja2 as novel interactor and regulator of PTP1B. Thus, praja2 ubiquitinates PTP1B and sustains the insulin pathway, interfering with praja2 expression or activity negatively impacts on the insulin pathway. This different control mechanism of the insulin pathway through PTP1B ubiquitination adds a new dowel to the comprehension of the molecular basis of metabolic disorders.
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