Manck Raphael, Ishitsuka Yuji, Herrero Saturnino, Takeshita Norio, Nienhaus G Ulrich, Fischer Reinhard
Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Department of Microbiology, Hertzstrasse 16, Karlsruhe D-76187, Germany.
Karlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Physics and Center for Functional Nanostructures, Karlsruhe 76131, Germany.
J Cell Sci. 2015 Oct 1;128(19):3569-82. doi: 10.1242/jcs.169094. Epub 2015 Aug 13.
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.
真核生物中细胞从对称向极性的转变依赖于微管(MT)和肌动蛋白细胞骨架。在诸如粟酒裂殖酵母或构巢曲霉等真菌中,MT细胞骨架通过皮层细胞末端标记蛋白来确定肌动蛋白聚合的位点。在此,我们将构巢曲霉的MT引导蛋白A(MigA)描述为丝状真菌中酿酒酵母核融合蛋白Kar9的首个直系同源物。构巢曲霉的MigA与皮层ApsA蛋白相互作用,并在有丝分裂期间参与纺锤体定位。MigA还与隔膜和核MT组织中心(MTOC)相关联。超分辨率光激活定位显微镜(PALM)分析表明,MigA以依赖EbA的方式被招募到正在组装和回缩的MT正端。MigA是菌丝尖端MT汇聚所必需的,并且在细胞末端标记物TeaA和TeaR的正确定位中发挥作用。此外,MigA与V类肌球蛋白相互作用,这表明存在一种主动机制来捕获MT并沿着肌动蛋白丝拉动其末端。因此,MT和肌动蛋白的组织相互依赖,正反馈回路确保了强劲的极性生长。