Porpora, Monia (2014) Identification of pericentriolar matrix protein 1 (PCM1) as a novel scaffold for Protein Kinase A (PKA) and NIMA-related kinase 10 (NEK10). [Tesi di dottorato]

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Tipologia del documento: Tesi di dottorato
Lingua: English
Titolo: Identification of pericentriolar matrix protein 1 (PCM1) as a novel scaffold for Protein Kinase A (PKA) and NIMA-related kinase 10 (NEK10)
Autori:
AutoreEmail
Porpora, Moniamonia.porpora@hotmail.it
Data: 31 Marzo 2014
Numero di pagine: 80
Istituzione: Università degli Studi di Napoli Federico II
Dipartimento: Medicina Molecolare e Biotecnologie Mediche
Scuola di dottorato: Medicina molecolare
Dottorato: Patologia e fisiopatologia molecolare
Ciclo di dottorato: 26
Coordinatore del Corso di dottorato:
nomeemail
Avvedimento, Vittorio Enricovittorioenrico.avvedimento@unina.it
Tutor:
nomeemail
Feliciello, Antonio[non definito]
Data: 31 Marzo 2014
Numero di pagine: 80
Parole chiave: PCM1;PKA;NEK10
Settori scientifico-disciplinari del MIUR: Area 06 - Scienze mediche > MED/04 - Patologia generale
Depositato il: 10 Apr 2014 13:24
Ultima modifica: 17 Mag 2017 01:00
URI: http://www.fedoa.unina.it/id/eprint/9893

Abstract

The pericentriolar material 1 (PCM1) assembles a molecular platform around the pericentriolar matrix and centrosome that is essential for cell division and microtubule dynamics, and plays a critical role in different aspects of mitosis and ciliogenesis. Here, we report an additonal layer of complexity and found that PCM1 nucleates a signaling complex at the pericentriolar matrix, which includes PKA and NEK10. By co-clustering two distinct signaling enzymes, PCM1 controls critical aspects of mammalian ciliogenesis. Within the PCM1 complex, PKA regulates NEK10 localization and stability, efficiently coupling cAMP signaling to the ubiquitin-proteasome system (UPS). In this context, PCM1 acts as relay that senses, transmits and integrates cAMP and mitogenic signals generated at cell membrane, regulating biological events at the pericentriolar matrix area and primary cilium. The molecular characterization of relevant protein complexes at specific sub-cellular compartments and understanding the role of scaffold platform in critical aspects of cell biology will likely contribute to the design of novel therapeutic approaches for human diseases.

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