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NADPH oxidases regulate septin-mediated cytoskeletal remodeling during plant infection by the rice blast fungus.


ABSTRACT: The rice blast fungus Magnaporthe oryzae infects plants with a specialized cell called an appressorium, which uses turgor to drive a rigid penetration peg through the rice leaf cuticle. Here, we show that NADPH oxidases (Nox) are necessary for septin-mediated reorientation of the F-actin cytoskeleton to facilitate cuticle rupture and plant cell invasion. We report that the Nox2-NoxR complex spatially organizes a heteroligomeric septin ring at the appressorium pore, required for assembly of a toroidal F-actin network at the point of penetration peg emergence. Maintenance of the cortical F-actin network during plant infection independently requires Nox1, a second NADPH oxidase, which is necessary for penetration hypha elongation. Organization of F-actin in appressoria is disrupted by application of antioxidants, whereas latrunculin-mediated depolymerization of appressorial F-actin is competitively inhibited by reactive oxygen species, providing evidence that regulated synthesis of reactive oxygen species by fungal NADPH oxidases directly controls septin and F-actin dynamics.

SUBMITTER: Ryder LS 

PROVIDER: S-EPMC3581893 | biostudies-other | 2013 Feb

REPOSITORIES: biostudies-other

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NADPH oxidases regulate septin-mediated cytoskeletal remodeling during plant infection by the rice blast fungus.

Ryder Lauren S LS   Dagdas Yasin F YF   Mentlak Thomas A TA   Kershaw Michael J MJ   Thornton Christopher R CR   Schuster Martin M   Chen Jisheng J   Wang Zonghua Z   Talbot Nicholas J NJ  

Proceedings of the National Academy of Sciences of the United States of America 20130204 8


The rice blast fungus Magnaporthe oryzae infects plants with a specialized cell called an appressorium, which uses turgor to drive a rigid penetration peg through the rice leaf cuticle. Here, we show that NADPH oxidases (Nox) are necessary for septin-mediated reorientation of the F-actin cytoskeleton to facilitate cuticle rupture and plant cell invasion. We report that the Nox2-NoxR complex spatially organizes a heteroligomeric septin ring at the appressorium pore, required for assembly of a tor  ...[more]

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