Dynamic assembly of a higher-order septin structure during appressorium morphogenesis by the rice blast fungus

Dulal, Nawaraj; Rogers, Audra Mae; Wang, Yong; Egan, Martin J.

doi:10.1016/j.fgb.2020.103385

Cited by 22 publications

(26 citation statements)

References 30 publications

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“…Importantly, improved understanding of this process in M. oryzae could provide new clues into the regulation of septin assembly in diverse systems (Bridges and Gladfelter, 2015). Previously, we showed that septin structures undergo remodeling from an incipient disc to a toroidal ring during appressorium development (Dulal et al, 2020). Here, we provide evidence that this septin disc-to-ring transitions is driven, in part, by dynamic remodeling of the F-actin cytoskeleton in M. oryzae.…”

Section: Introductionmentioning

confidence: 59%

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Turgor-dependent and coronin-mediated F-actin dynamics drive septin disc-to-ring remodeling in the blast fungus Magnaporthe oryzae

Dulal

Rogers

Proko

et al. 2021

Journal of Cell Science

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The fungus Magnaporthe oryzae uses a specialized pressure-generating infection cell called an appressorium to break into rice leaves and initiate disease. Appressorium functionality is dependent on the formation of a cortical septin ring during its morphogenesis, but precisely how this structure assembles is unclear. Here we show that F-actin rings are recruited to the circumference of incipient septin disc-like structures in a pressure-dependent manner, and that this is necessary for their contraction and remodeling into rings. We demonstrate that the structural integrity of these incipient septin discs requires both an intact F-actin and microtubule cytoskeleton and provide fundamental new insight into their functional organization within the appressorium. Lastly, using proximity-dependent, labelling we identify the actin modulator coronin as a septin proximal protein and show that F-actin-mediated septin disc-to-ring remodeling is perturbed in the genetic absence of coronin. Taken together, our findings provide new insight into the dynamic remodeling of infection-specific higher-order septin structures in a globally significant fungal plant pathogen.

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Section: Introductionmentioning

confidence: 59%

“…1A,B). Imaging revealed that an F-actin ring forms around the circumference of an incipient septin disc soon after septation in the appressorium neck (Saunders et al, 2010b;Dulal et al, 2020) (Fig. 1A; Movie 1).…”

Section: Resultsmentioning

confidence: 99%

Turgor-dependent and coronin-mediated F-actin dynamics drive septin disc-to-ring remodeling in the blast fungus Magnaporthe oryzae

Dulal

Rogers

Proko

et al. 2021

Journal of Cell Science

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“…During the establishment of disease, microbial pathogens like M. oryzae are exposed to diverse cellular stressors, which can cause damage to their proteome and the formation of toxic misfolded protein conformers. An important and broadly conserved (Veneault-Fourrey et al, 2006;Saunders et al, 2010b;Dagdas et al, 2012;Dulal et al, 2020). (B, C) Plots showing a time course of the number of Hsp104-positive aggregates present in conidia (B), and fully mature appressoria (C), following recovery from heat shock.…”

Section: Introductionmentioning

confidence: 99%

“…FIGURE 1: Hsp104-positive protein aggregates are cleared during infection-related development. (A) Cartoon depicting relevant morphogenetic landmarks associated with appressorium development by M. oryzae, based on previous observations(Veneault-Fourrey et al, 2006;Saunders et al, 2010b;Dagdas et al, 2012;Dulal et al, 2020). (B, C) Plots showing a time course of the number of Hsp104-positive aggregates present in conidia (B), and fully mature appressoria (C), following recovery from heat shock.…”

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confidence: 99%

Autophagy machinery promotes the chaperone-mediated formation and compartmentalization of protein aggregates during appressorium development by the rice blast fungus

Rogers

Egan

2020

MBoC

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The chaperone-mediated sequestration of misfolded proteins into specialized quality control compartments represents an important strategy for maintaining protein homeostasis in response to stress. However, precisely how this process is controlled in time and subcellular space and integrated with the cell's protein refolding and degradation pathways, remains unclear. We set out to understand how aggregated proteins are managed during infection-related development by a globally devastating plant pathogenic fungus, and to determine how impaired protein quality control impacts upon cellular differentiation and pathogenesis in this system. Here we show that in the absence of Hsp104 disaggregase activity aggregated proteins are spatially sequestered into quality control compartments within conidia, but not within terminally differentiated infection cells, and thus spatial protein quality control is cell-type dependent. We demonstrate that impaired aggregate resolution results in a short-term developmental penalty but has no significant impact upon appressorium function. Lastly, we show that, somewhat unexpectedly, the autophagy machinery is necessary for the normal formation and compartmentalization of protein aggregates. Taken together, our findings provide important new insight into spatial protein quality control during the process of terminal cellular differentiation by a globally important model eukaryote and reveals a new level of interplay between major proteostasis pathways. [Media: see text]

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“…De longe, as septinas de levedura e septinas humanas são as mais bem estudadas. [6][7] Porém, estudos em septinas de outros organismos estão começando a ter maior ênfase, destacando septinas de: fungos fitopatogênicos [8][9][10] , Caenorhabditis elegans [11][12] , Schistosoma mansoni 13,14, , Drosophila melanogaster [15][16] e Mus musculus. [17][18] Figura 2 -Distribuição filogenética de septinas nos organismos eucariotos.…”

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Determinantes estruturais para a especificidade de interação nas interfaces G e NC de septinas: validando as regras de substituição na montagem do filamento

Leonardo¹

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Agradeço ao meu orientador e amigo o Prof. Dr. Richard Charles Garratt por me dar a oportunidade de fazer parte do seu grupo de pesquisa desde o ano 2012, formando-me como cientista desde minha iniciação científica até o meu doutorado. Obrigado pelas horas de estudo e discussão durante o desenvolvimento deste projeto, e por ser um professor e cientista exemplar. Aos professores do IFSC que contribuíram para a minha formação cientifica, especialmente a Prof a . Dr a . Ana Paula Ulian de Araújo e o Prof. Dr. Ricardo De Marco pelas sugestões e discussões para melhorar o meu trabalho de pesquisa. Aos técnicos do Laboratório de Biologia Estrutural: Humberto e Susana, e aos técnicos do Grupo de Biofísica Molecular: Andressa, Bel e Rafael, pelo constante apoio nos diversos experimentos assim como por sua amizade. A meus colegas do grupo de septinas pelas sugestões e discussões durante as reuniões de

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Dynamic assembly of a higher-order septin structure during appressorium morphogenesis by the rice blast fungus

Cited by 22 publications

References 30 publications

Turgor-dependent and coronin-mediated F-actin dynamics drive septin disc-to-ring remodeling in the blast fungus Magnaporthe oryzae

Turgor-dependent and coronin-mediated F-actin dynamics drive septin disc-to-ring remodeling in the blast fungus Magnaporthe oryzae

Autophagy machinery promotes the chaperone-mediated formation and compartmentalization of protein aggregates during appressorium development by the rice blast fungus

Determinantes estruturais para a especificidade de interação nas interfaces G e NC de septinas: validando as regras de substituição na montagem do filamento

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