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Genetic evidence for a microtubule-capture mechanism during polarised growth of Aspergillus nidulans.
Manck, Raphael; Ishitsuka, Yuji; Herrero, Saturnino; Takeshita, Norio; Nienhaus, G Ulrich; Fischer, Reinhard.
Afiliação
  • Manck R; Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Department of Microbiology, Hertzstrasse 16, Karlsruhe D-76187, Germany.
  • Ishitsuka Y; Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Physics and Center for Functional Nanostructures, Karlsruhe 76131, Germany.
  • Herrero S; Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Department of Microbiology, Hertzstrasse 16, Karlsruhe D-76187, Germany.
  • Takeshita N; Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Department of Microbiology, Hertzstrasse 16, Karlsruhe D-76187, Germany University of Tsukuba, Faculty of Life and Environmental Sciences, Tsukuba, Ibaraki 305-8572, Japan.
  • Nienhaus GU; Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Physics and Center for Functional Nanostructures, Karlsruhe 76131, Germany.
  • Fischer R; Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Department of Microbiology, Hertzstrasse 16, Karlsruhe D-76187, Germany reinhard.fischer@kit.edu.
J Cell Sci ; 128(19): 3569-82, 2015 Oct 01.
Article em En | MEDLINE | ID: mdl-26272919
ABSTRACT
The cellular switch from symmetry to polarity in eukaryotes depends on the microtubule (MT) and actin cytoskeletons. In fungi such as Schizosaccharomyces pombe or Aspergillus nidulans, the MT cytoskeleton determines the sites of actin polymerization through cortical cell-end marker proteins. Here we describe A. nidulans MT guidance protein A (MigA) as the first ortholog of the karyogamy protein Kar9 from Saccharomyces cerevisiae in filamentous fungi. A. nidulans MigA interacts with the cortical ApsA protein and is involved in spindle positioning during mitosis. MigA is also associated with septal and nuclear MT organizing centers (MTOCs). Super-resolution photoactivated localization microscopy (PALM) analyses revealed that MigA is recruited to assembling and retracting MT plus ends in an EbA-dependent manner. MigA is required for MT convergence in hyphal tips and plays a role in correct localization of the cell-end markers TeaA and TeaR. In addition, MigA interacts with a class-V myosin, suggesting that an active mechanism exists to capture MTs and to pull the ends along actin filaments. Hence, the organization of MTs and actin depend on each other, and positive feedback loops ensure robust polar growth.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspergillus nidulans / Proteínas Fúngicas / Centro Organizador dos Microtúbulos Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspergillus nidulans / Proteínas Fúngicas / Centro Organizador dos Microtúbulos Idioma: En Ano de publicação: 2015 Tipo de documento: Article