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Inheritance of the Golgi Apparatus and Cytokinesis Are Controlled by Degradation of GBF1.
Magliozzi, Roberto; Carrero, Zunamys I; Low, Teck Yew; Yuniati, Laurensia; Valdes-Quezada, Christian; Kruiswijk, Flore; van Wijk, Koen; Heck, Albert J R; Jackson, Catherine L; Guardavaccaro, Daniele.
Afiliação
  • Magliozzi R; Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 Utrecht, the Netherlands.
  • Carrero ZI; Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 Utrecht, the Netherlands.
  • Low TY; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 Utrecht, the Netherlands; The Netherlands Proteomics Center, Padualaan 8, 3584 Utrecht, the Netherlands.
  • Yuniati L; Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 Utrecht, the Netherlands.
  • Valdes-Quezada C; Oncode Institute, Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 Utrecht, the Netherlands.
  • Kruiswijk F; Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 Utrecht, the Netherlands.
  • van Wijk K; Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 Utrecht, the Netherlands.
  • Heck AJR; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 Utrecht, the Netherlands; The Netherlands Proteomics Center, Padualaan 8, 3584 Utrecht, the Netherlands.
  • Jackson CL; Membrane Dynamics and Intracellular Trafficking, Institut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013 Paris, France.
  • Guardavaccaro D; Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 Utrecht, the Netherlands. Electronic address: d.guardavaccaro@hubrecht.eu.
Cell Rep ; 23(11): 3381-3391.e4, 2018 06 12.
Article em En | MEDLINE | ID: mdl-29898406
Although much is known about how chromosome segregation is coupled to cell division, how intracellular organelles partition during mitotic division is poorly understood. We report that the phosphorylation-dependent degradation of the ARFGEF GBF1 regulates organelle trafficking during cell division. We show that, in mitosis, GBF1 is phosphorylated on Ser292 and Ser297 by casein kinase-2 allowing recognition by the F-box protein ßTrCP. GBF1 interaction with ßTrCP recruits GBF1 to the SCFßTrCP ubiquitin ligase complex, triggering its degradation. Phosphorylation and degradation of GBF1 occur along microtubules at the intercellular bridge of telophase cells and are required for Golgi membrane positioning and postmitotic Golgi reformation. Indeed, expression of a non-degradable GBF1 mutant inhibits the transport of the Golgi cluster adjacent to the midbody toward the Golgi twin positioned next to the centrosome and results in defective Golgi reassembly and cytokinesis failure. These findings define a mechanism that controls postmitotic Golgi reassembly and inheritance.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fatores de Troca do Nucleotídeo Guanina / Citocinese / Complexo de Golgi Limite: Humans Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fatores de Troca do Nucleotídeo Guanina / Citocinese / Complexo de Golgi Limite: Humans Idioma: En Ano de publicação: 2018 Tipo de documento: Article