Cla4 PAK-like kinase is required for pathogenesis, asexual/sexual development and polarized growth in Bipolaris maydis

Kitade, Yuki; Sumita, Takuya; Izumitsu, Kosuke; Tanaka, Chihiro

doi:10.1007/s00294-019-00977-9

Cited by 10 publications

(13 citation statements)

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“…Further, ∆cla4 exhibits dense growth and altered branching in vegetative hyphae, suggesting that CLA4 is involved in regulating cell polarity in S. macrospora . This observation is consistent to reports by others, thus indicating that CLA4 function is conserved in filamentous ascomycetes (Kitade et al, ; Lichius et al, ; Rolke & Tudzynski, ; Tian, Zhou, Guo, & Wang, ). The branching pattern of hyphae might be due to the nonregular distribution of the Spitzenkörper, as was suggested for a B. maydis ∆cla4 deletion strain (Kitade et al, ).…”

Section: Discussionsupporting

confidence: 93%

“…This observation is consistent to reports by others, thus indicating that CLA4 function is conserved in filamentous ascomycetes (Kitade et al, 2019;Lichius et al, 2014;Rolke & Tudzynski, 2008;Tian, Zhou, Guo, & Wang, 2015). The branching pattern of hyphae might be due to the nonregular distribution of the Spitzenkörper, as was suggested for a B. maydis ∆cla4 deletion strain (Kitade et al, 2019). In S. cerevisiae, the PAK1 homolog Cla4p has also been extensively investigated.…”

Section: Phosphorylation Of the Potential Stripak Target Cla4 Controls Fungal Developmentsupporting

confidence: 91%

“…This finding is similar to previous reports that have investigated the function of CLA4 homologs in other filamentous fungi. For example, in Bipolaris maydis, the CLA4 homolog regulates the formation of fruiting bodies as well as ascospore development (Kitade, Sumita, Izumitsu, & Tanaka, 2019). Similarly, CLA4 homologs in F. graminaerum, N. crassa and M. grisea affect ascospore development and release, but not fruiting body morphology (Li, Xue, Bruno, Nishimura, & Xu, 2004;Park et al, 2011;Wang et al, 2011).…”

Section: Phosphorylation Of the Potential Stripak Target Cla4 Controls Fungal Developmentmentioning

confidence: 99%

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Phosphoproteomic analysis of STRIPAK mutants identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important in fungal sexual development and polarized growth

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Beier-Rosberger

et al. 2020

Molecular Microbiology

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The highly conserved striatin‐interacting phosphatases and kinases (STRIPAK) complex regulates phosphorylation/dephosphorylation of developmental proteins in eukaryotic microorganisms, animals and humans. To first identify potential targets of STRIPAK, we performed extensive isobaric tags for relative and absolute quantification‐based proteomic and phosphoproteomic analyses in the filamentous fungus Sordaria macrospora. In total, we identified 4,193 proteins and 2,489 phosphoproteins, which are represented by 10,635 phosphopeptides. By comparing phosphorylation data from wild type and mutants, we identified 228 phosphoproteins to be regulated in all three STRIPAK mutants, thus representing potential targets of STRIPAK. To provide an exemplarily functional analysis of a STRIPAK‐dependent phosphorylated protein, we selected CLA4, a member of the conserved p21‐activated kinase family. Functional characterization of the ∆cla4 deletion strain showed that CLA4 controls sexual development and polarized growth. To determine the functional relevance of CLA4 phosphorylation and the impact of specific phosphorylation sites on development, we next generated phosphomimetic and ‐deficient variants of CLA4. This analysis identified (de)phosphorylation of a highly conserved serine (S685) residue in the catalytic domain of CLA4 as being important for fungal cellular development. Collectively, these analyses significantly contribute to the understanding of the mechanistic function of STRIPAK as a phosphatase and kinase signaling complex.

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Section: Discussionsupporting

confidence: 93%

Section: Phosphorylation Of the Potential Stripak Target Cla4 Controls Fungal Developmentsupporting

confidence: 91%

Section: Phosphorylation Of the Potential Stripak Target Cla4 Controls Fungal Developmentmentioning

confidence: 99%

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Phosphoproteomic analysis of STRIPAK mutants identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important in fungal sexual development and polarized growth

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Blank-Landeshammer

Beier-Rosberger

et al. 2020

Molecular Microbiology

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“…Further, Δcla4 exhibits dense growth and altered branching in vegetative hyphae, suggesting that CLA4 is involved in regulating cell polarity in S. macrospora . This observation is consistent to reports by others, thus indicating that CLA4 function is conserved in filamentous ascomycetes (Rolke and Tudzynski 2008; Lichius et al 2014; Tian et al 2015; Kitade et al 2019). The branching pattern of hyphae might be due to the non-regular distribution of the Spitzenkörper, as was suggested for a B. maydis Δcla4 deletion strain (Kitade et al 2019).…”

Section: Discussionsupporting

confidence: 93%

“…This finding is similar to previous reports that have investigated the function of CLA4 homologues in other filamentous fungi. For example, in Bipolaris maydis , the CLA4 homologue regulates the formation of fruiting bodies as well as ascospore development (Kitade et al 2019). Similarly, CLA4 homologues in F. graminaerum , N. crassa , and M. grisea affect ascospore development and release, but not fruiting body morphology (Li et al 2004; Park et al 2011; Wang et al 2011).…”

Section: Discussionmentioning

confidence: 99%

iTRAQ-based proteomic and phosphoproteomic analyses of STRIPAK mutants from the fungusSordaria macrosporaidentifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important for sexual development and polarized growth

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Blank-Landeshammer

Beier-Rosberger

et al. 2019

Preprint

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1 from the fungus Sordaria macrospora identifies a conserved serine phosphorylation 2 site in PAK kinase CLA4 to be important for sexual development and polarized 3 growth 4 5 6 Summary 22The highly conserved striatin-interacting phosphatases and kinases (STRIPAK) 23 complex regulates phosphorylation of developmental proteins in eukaryotic 24 microorganisms, animals, and humans. To first identify potential targets of 25 STRIPAK, we performed extensive isobaric tags for relative and absolute 26 quantification (iTRAQ)-based proteomic and phosphoproteomic analyses in the 27 filamentous fungus Sordaria macrospora. In total, we identified 4,193 proteins and 28 2,489 phosphoproteins, which are represented by 10,635 phosphopeptides. By 29 comparing phosphorylation data from wild-type and mutants, we identified 228 30 phosphoproteins to be regulated in all three STRIPAK mutants, thus representing 31 potential targets of STRIPAK. To provide an exemplarily functional analysis of a 32 STRIPAK-dependent phosphorylated protein, we selected CLA4, a member of the 33 conserved p21-activated kinase (PAK) family. Functional characterization of the 34 ∆cla4 deletion strain showed that CLA4 controls sexual development and polarized 35 growth. To determine the functional relevance of CLA4 phosphorylation and the 36 impact of specific phosphorylation sites on development, we next generated 37 phospho-mimetic and -deficient variants of CLA4. This analysis identified 38 (de)phosphorylation of a highly conserved serine (S685) residue in the catalytic 39 domain of CLA4 as being important for fungal cellular development. Collectively, 40 these analyses significantly contribute to the understanding of the mechanistic 41 function of STRIPAK as a phosphatase and kinase signaling complex. 42 43 44 45 46 Results 102 In this work, detailed iTRAQ-based proteomic and phosphoproteomic analyses of 103 the wild-type and three different STRIPAK deletion strains led to the identification of 104 putative dephosphorylation targets of the STRIPAK complex in S. macrospora. 105 Importantly, functional characterization of the PAK kinase CLA4, a target protein of 106 STRIPAK deciphers their role in fungal cellular development. 107 108 iTRAQ-based proteomic and phosphoproteomic analyses revealed putative 109 dephosphorylation targets of the STRIPAK complex 110 To identify dephosphorylation targets of STRIPAK, we performed iTRAQ-based LC-111 MS/MS proteomic and phosphoproteomic analyses to directly compare relative 112 changes in protein expression (Fig. 1). The iTRAQ strategy is based on the N-113 terminal labelling of peptides with up to eight amino group-reactive reagents coupled 114 to different reporter and balancer groups (Ross et al. 2004; Wu et al. 2006). Thus, 115 we were able to conduct a simultaneous analysis of up to eight different cultural 116 samples. While these isobaric tags have the same mass, fragmentation during 117 tandem MS (MS/MS) leads to the generation of mass-specific reporter ions whose 118 abundances are used for protein quantific...

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An efficient targeted gene deletion approach for Cochliobolus heterostrophus using Agrobacterium tumefaciens-mediated transformation

Sun,

Yang,

Liu

et al. 2024

Journal of Microbiological Methods

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Cla4 PAK-like kinase is required for pathogenesis, asexual/sexual development and polarized growth in Bipolaris maydis

Cited by 10 publications

References 45 publications

Phosphoproteomic analysis of STRIPAK mutants identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important in fungal sexual development and polarized growth

Phosphoproteomic analysis of STRIPAK mutants identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important in fungal sexual development and polarized growth

iTRAQ-based proteomic and phosphoproteomic analyses of STRIPAK mutants from the fungusSordaria macrosporaidentifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important for sexual development and polarized growth

An efficient targeted gene deletion approach for Cochliobolus heterostrophus using Agrobacterium tumefaciens-mediated transformation

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