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• W1887630037 abstract "Polar morphogenesis is required for the function of elongated cell types like neuronal cells, pollen tubes and cells of filamentous fungi. The basal signalling components involved are highly conserved. Defects in polar cell shape can result in developmental disorders or death of the affected cell. In this work two components involved in polar growth were analysed at a molecular level in Neurospora crassa. These are LRG1, which is a member of the GTPase activating proteins (GAPs), and the germinal center kinase POD6.POD6 and LRG1 are proteins essential for hyphal tip elongation. Deletion and temperature sensitive mutants of pod-6 and lrg-1 show phenotypic similarities to cot-1 temperature sensitive mutant in cessation of hyphal elongation and excessive hyperbranching. All three proteins are also involved in determining the size of hyphal compartments. Complementation analysis revealed that both parts, the N-terminal containing three LIM domains as well as the C-terminal harbouring the Rho GAP domain of LRG1, are required for its function. Genetic evidence and in vitro GTPase assays identify LRG1 as a RHO1 specific GAP. Localisation experiments revealed a partial colocalisation of POD6 and COT1 that depends on the oppositely directed microtubule motor proteins kinesin-1 and dynein. LRG1 shows a similar localisation and is enriched at septae and at hyphal tips. This was observed by immunofluorescence studies with antibodies generated against LRG1 and confirmed in a strain expressing MYC9::LRG1. In strains expressing GFP::LRG1, the dynamic accumulation of the fusion protein as an apical cap was observed. This localisation depends on the three LIM domains of LRG1, a functional actin cytoskeleton and active growth. Similar to the localisation of COT1 and POD6, LRG1 localisation is influenced by dynein and kinesin-1 and the microtubule cytoskeleton. LRG1 affects several output pathways of RHO1. Hyposensitivity of lrg-1(12-20) to the glucan synthase inhibitor caspofungin and synthetic lethality with a hyperactive ß1,3-glucan synthase mutant occurred. Further, suppression by the PKC inhibitors staurosporine and cercosporamide was observed. Hypersensitivity to the actin depolymerising drug latrunculin A and the suppression of defects in lrg-1 mutant strains by the overexpression of the dominant-negative acting N-terminus of the formin BNI1 indicate an influence on formin mediated actin polymerisation. In contrast, the cot-1 mutation has no influence regarding these RHO1 effectors. Taken together, these data suggest that LRG1 functions as a GAP for Rho1 that regulates several effector pathways. A complex of COT1 and POD6 acts in parallel to coordinate apical tip growth." @default.
• W1887630037 created "2016-06-24" @default.
• W1887630037 creator A5083298859 @default.
• W1887630037 date "2022-02-20" @default.
• W1887630037 modified "2023-10-01" @default.
• W1887630037 title "Governing fungal polar cell extension: Analysis of Rho GTPase and NDR kinase signalling in Neurospora crassa" @default.
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