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Hexameric NuMA:LGN structures promote multivalent interactions required for planar epithelial divisions.
Pirovano, Laura; Culurgioni, Simone; Carminati, Manuel; Alfieri, Andrea; Monzani, Silvia; Cecatiello, Valentina; Gaddoni, Chiara; Rizzelli, Francesca; Foadi, James; Pasqualato, Sebastiano; Mapelli, Marina.
Afiliação
  • Pirovano L; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
  • Culurgioni S; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
  • Carminati M; Exscientia Ltd., The Schröedinger Building, Heatley Road, Oxford Science Park, Oxford, OX4 4GE, UK.
  • Alfieri A; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
  • Monzani S; MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.
  • Cecatiello V; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
  • Gaddoni C; Department of Biosciences, Università degli Studi di Milano, 20133, Milan, Italy.
  • Rizzelli F; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
  • Foadi J; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
  • Pasqualato S; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
  • Mapelli M; IEO, European Institute of Oncology IRCCS, 20141, MILANO, Italy.
Nat Commun ; 10(1): 2208, 2019 05 17.
Article em En | MEDLINE | ID: mdl-31101817
ABSTRACT
Cortical force generators connect epithelial polarity sites with astral microtubules, allowing dynein movement to orient the mitotic spindle as astral microtubules depolymerize. Complexes of the LGN and NuMA proteins, fundamental components of force generators, are recruited to the cortex by Gαi-subunits of heterotrimeric G-proteins. They associate with dynein/dynactin and activate the motor activity pulling on astral microtubules. The architecture of cortical force generators is unknown. Here we report the crystal structure of NuMALGN hetero-hexamers, and unveil their role in promoting the assembly of active cortical dynein/dynactin motors that are required in orchestrating oriented divisions in polarized cells. Our work elucidates the basis for the structural organization of essential spindle orientation motors.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Polaridade Celular / Antígenos Nucleares / Proteínas Associadas à Matriz Nuclear / Peptídeos e Proteínas de Sinalização Intracelular / Fuso Acromático Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Polaridade Celular / Antígenos Nucleares / Proteínas Associadas à Matriz Nuclear / Peptídeos e Proteínas de Sinalização Intracelular / Fuso Acromático Idioma: En Ano de publicação: 2019 Tipo de documento: Article