Fcp-1 dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Fcp-1 dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit (Articolo in rivista) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

Alternative label

• Visconti R; Palazzo L; Della Monica R; Grieco D (2012)
  Fcp-1 dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit
  in Nature communications
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Visconti R; Palazzo L; Della Monica R; Grieco D (literal)

Pagina inizio

• 894 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 3 (literal)

Rivista

• Nature communications (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• R. Visconti= Istituto per l'Endocrinologia e l'Oncologia Sperimentale \"G. Salvatore\", Consiglio Nazionale delle Ricerche, Napoli, Italy. L. Palazzo; R. Della Monica; D. Grieco= CEINGE Biotecnologie Avanzate e Dipartimento di Biologia e Patologia Cellulare e Molecolare \"L. Califano\", Universita' degli Studi di Napoli \"Federico II\" (literal)

Titolo

• Fcp-1 dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit (literal)

Abstract

• Correct execution of mitosis in eukaryotes relies on timely activation and inactivation of cyclin B-dependent kinase 1 (cdk1), the M-phase-promoting factor (MPF). Once activated, MPF is sustained until mitotic spindle assembly by phosphorylation-dependent feedback loops that prevent inhibitory phosphorylation of cdk1 and ubiquitin-dependent degradation of cyclin B. Whether subsequent MPF inactivation and anaphase onset require a specific phosphatase(s) to reverse these feedback loops is not known. Here we show through biochemical and genetic evidence that timely MPF inactivation requires activity of the essential RNA polymerase II-carboxy-terminal domain phosphatase Fcp1, in a transcription-independent manner. We identify Cdc20, a coactivator of the ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C) required for cyclin degradation and anaphase onset, USP44, a deubiquitinating peptidase that opposes APC/C action, and Wee1, a cdk1 inhibitory kinase, as relevant Fcp1 targets. We propose that Fcp1 has a crucial role in the liaison between dephosphorylation and ubiquitination that drives mitosis exit. (literal)

Prodotto di

• Institute Experimental Endocrinology and Oncology \"Gaetano Salvatore\" (IEOS) (Istituto)
• Identificazione e caratterizzazione funzionale dei geni e delle proteine coinvolti nella tumorigenesi tiroidea (SV.P15.001.004) (Modulo)

Autore CNR

• ROBERTA VISCONTI (Persona)

Incoming links:

Autore CNR di

• ROBERTA VISCONTI (Persona)

Prodotto

• Institute Experimental Endocrinology and Oncology \"Gaetano Salvatore\" (IEOS) (Istituto)
• Identificazione e caratterizzazione funzionale dei geni e delle proteine coinvolti nella tumorigenesi tiroidea (SV.P15.001.004) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Nature communications (Rivista)