The rice blast fungus Magnaporthe oryzae differentiates a specialized infection structure called an appressorium, which is used to break into plant cells by directed application of enormous turgor force. Appressorium-mediated plant infection requires timely assembly of a higher-order septin ring structure at the base of the appressorium, which is needed to spatially orchestrate appressorium repolarization. Here we use quantitative 4D widefield fluorescence imaging to gain new insight into the spatiotemporal dynamics of septin ring formation, and septin-mediated actin re-organization, during appressorium morphogenesis by M. oryzae. We anticipate that the new knowledge will provide a quantitative framework for dissecting the molecular mechanisms of higher-order septin ring assembly in this devastating plant pathogenic fungus.
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http://dx.doi.org/10.1016/j.fgb.2020.103385 | DOI Listing |
Curr Opin Cell Biol
December 2024
Institute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany. Electronic address:
Septins are involved in many important cellular processes, and septin dysfunction has been implicated in various pathologies, such as cancer. Like other components of the cytoskeleton -F-actin, microtubules, and intermediate filaments-septins can self-assemble into filaments and higher-order structures. These non-polar filaments are assembled from complex and variable multimeric building blocks.
View Article and Find Full Text PDFMol Biol Cell
October 2024
Department of Cell Biology, Duke University School of Medicine, Durham, NC 27708.
Morphological complexity and plasticity are hallmarks of polyextremotolerant fungi. Septins are conserved cytoskeletal proteins and key contributors to cell polarity and morphogenesis. They sense membrane curvature, coordinate cell division, and influence diffusion at the plasma membrane.
View Article and Find Full Text PDFCold Spring Harb Perspect Biol
December 2024
Department of Cell Biology, Duke University, Durham, North Carolina 27708, USA
This review examines the relationships between membrane chemistry, curvature-sensing proteins, and cellular morphogenesis. Curvature-sensing proteins are often orders of magnitude smaller than the membrane curvatures they localize to. How are nanometer-scale proteins used to sense micrometer-scale membrane features? Here, we trace the journey of curvature-sensing proteins as they engage with lipid membranes through a combination of electrostatic and hydrophobic interactions.
View Article and Find Full Text PDFBiosci Rep
March 2024
Jeffrey Cheah School of Medicine and Health Sciences, Monash University Malaysia, Bandar Sunway 47500, Selangor, Malaysia.
Septin proteins are a subfamily of closely related GTP-binding proteins conserved in all species except for higher plants and perform essential biological processes. Septins self-assemble into heptameric or octameric complexes and form higher-order structures such as filaments, rings, or gauzes by end-to-end binding. Their close association with cell membrane components makes them central in regulating critical cellular processes.
View Article and Find Full Text PDFCommun Biol
January 2024
Institute of Molecular Genetics and Cell Biology, Ulm University, Ulm, Germany.
The septins of the yeast Saccharomyces cerevisiae assemble into hetero-octameric rods by alternating interactions between neighboring G-domains or N- and C-termini, respectively. These rods polymerize end to end into apolar filaments, forming a ring beneath the prospective new bud that expands during the cell cycle into an hourglass structure. The hourglass finally splits during cytokinesis into a double ring.
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