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14-3-3γ prevents centrosome duplication by inhibiting NPM1 function.
Bose, Arunabha; Modi, Kruti; Dey, Suchismita; Dalvi, Somavally; Nadkarni, Prafful; Sudarshan, Mukund; Kundu, Tapas K; Venkatraman, Prasanna; Dalal, Sorab N.
Afiliação
  • Bose A; Advanced Centre for Treatment Research and Education in Cancer (ACTREC), Tata Memorial Centre, Navi Mumbai, India.
  • Modi K; Homi Bhabha National Institute, Mumbai, India.
  • Dey S; Advanced Centre for Treatment Research and Education in Cancer (ACTREC), Tata Memorial Centre, Navi Mumbai, India.
  • Dalvi S; Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore, India.
  • Nadkarni P; Advanced Centre for Treatment Research and Education in Cancer (ACTREC), Tata Memorial Centre, Navi Mumbai, India.
  • Sudarshan M; Advanced Centre for Treatment Research and Education in Cancer (ACTREC), Tata Memorial Centre, Navi Mumbai, India.
  • Kundu TK; Advanced Centre for Treatment Research and Education in Cancer (ACTREC), Tata Memorial Centre, Navi Mumbai, India.
  • Venkatraman P; Homi Bhabha National Institute, Mumbai, India.
  • Dalal SN; Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore, India.
Genes Cells ; 26(6): 426-446, 2021 Jun.
Article em En | MEDLINE | ID: mdl-33813791
ABSTRACT
14-3-3 proteins bind to ligands via phospho-serine containing consensus motifs. However, the molecular mechanisms underlying complex formation and dissociation between 14-3-3 proteins and their ligands remain unclear. We identified two conserved acidic residues in the 14-3-3 peptide-binding pocket (D129 and E136) that potentially regulate complex formation and dissociation. Altering these residues to alanine led to opposing effects on centrosome duplication. D129A inhibited centrosome duplication, whereas E136A stimulated centrosome amplification. These results were due to the differing abilities of these mutant proteins to form a complex with NPM1. Inhibiting complex formation between NPM1 and 14-3-3γ led to an increase in centrosome duplication and over-rode the ability of D129A to inhibit centrosome duplication. We identify a novel role of 14-3-3γ in regulating centrosome licensing and a novel mechanism underlying the formation and dissociation of 14-3-3 ligand complexes dictated by conserved residues in the 14-3-3 family.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopeptídeos / Proteínas Nucleares / Centrossomo / Proteínas 14-3-3 Limite: Humans Idioma: En Revista: Genes Cells Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Índia

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopeptídeos / Proteínas Nucleares / Centrossomo / Proteínas 14-3-3 Limite: Humans Idioma: En Revista: Genes Cells Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Índia
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