Chiuso, Francesco (2017) Regulation of PTP1B stability and signaling by the PKA scaffold protein praja2. [Tesi di dottorato]

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Item Type: Tesi di dottorato
Lingua: English
Title: Regulation of PTP1B stability and signaling by the PKA scaffold protein praja2
Creators:
CreatorsEmail
Chiuso, Francescofrancesco.chiuso@gmail.com
Date: 10 December 2017
Number of Pages: 57
Institution: Università degli Studi di Napoli Federico II
Department: dep14
Dottorato: phd054
Ciclo di dottorato: 30
Coordinatore del Corso di dottorato:
nomeemail
Avvedimento, Vittorio Enricovittorioenrico.avvedimento@unina.it
Tutor:
nomeemail
Feliciello, AntonioUNSPECIFIED
Date: 10 December 2017
Number of Pages: 57
Uncontrolled Keywords: praja2 PTP1B PKA cAMP UPS
Settori scientifico-disciplinari del MIUR: Area 06 - Scienze mediche > MED/04 - Patologia generale
Date Deposited: 27 Dec 2017 17:16
Last Modified: 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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