Abstract
Dynamins are large superfamily GTPase proteins that are involved in various cellular processes including budding of transport vesicles, division of organelles, cytokinesis, and pathogen resistance. Here, we characterized several dynamin-related proteins from the rice blast fungus Magnaporthe oryzae and found that MoDnm1 is required for normal functions, including vegetative growth, conidiogenesis, and full pathogenicity. In addition, we found that MoDnm1 co-localizes with peroxisomes and mitochondria, which is consistent with the conserved role of dynamin proteins. Importantly, MoDnm1-dependent peroxisomal and mitochondrial fission involves functions of mitochondrial fission protein MoFis1 and WD-40 repeat protein MoMdv1. These two proteins display similar cellular functions and subcellular localizations as MoDnm1, and are also required for full pathogenicity. Further studies showed that MoDnm1, MoFis1 and MoMdv1 are in complex to regulate not only peroxisomal and mitochondrial fission, pexophagy and mitophagy progression, but also appressorium function and host penetration. In summary, our studies provide new insights into how MoDnm1 interacts with its partner proteins to mediate peroxisomal and mitochondrial functions and how such regulatory events may link to differentiation and pathogenicity in the rice blast fungus.
Highlights
Dynamins are large GTPase superfamily proteins that are involved in scission of nascent vesicles from parent membranes in eukaryotic cells [1]
In addition to revealing major conserved dynamin functions, we described how MoDnm1 interacts with mitochondrial fission protein MoFis1 and WD repeat adaptor protein MoMdv1 to mediate peroxisomal and mitochondrial fission, pexophagy and mitophagy
Dynamins and dynamin-related proteins (DRPs) participate in a wide variety of cellular processes, including budding mitochondrial fission and fusion, vacuolar fission (S. cerevisiae Vps1), interferon-induced anti-viral protection, plant cell cytokinesis and membrane fission (Arabidopsis thaliana DRP proteins), as well as pathogen resistance [1, 6]
Summary
Dynamins are large GTPase superfamily proteins that are involved in scission (cleavage of the vesicle from the parent membrane) of nascent vesicles from parent membranes in eukaryotic cells [1]. Dynamins and DRPs participate in a wide variety of cellular processes, including budding mitochondrial fission (mammalian Dlp and Saccharomyces cerevisiae Dnm1) and fusion (mammalian OPA1, S. cerevisiae Mgm and Schizosaccharomyces pombe Msp1), vacuolar fission (S. cerevisiae Vps1), interferon-induced anti-viral protection (fish Mx proteins), plant cell cytokinesis and membrane fission (Arabidopsis thaliana DRP proteins), as well as pathogen resistance [1, 6]. Among two groups of peroxisomal proteins that have a pronounced influence on peroxisome size and abundance, DRPs are required for the scission of peroxisomal membranes [13], while Pex11-type peroxisome proliferators are involved in the proliferation of peroxisomes [14,15,16]. The DRP involvement in peroxisomal fission has been found in plants. In A. thaliana DRP3A mutants, peroxisomes are elongated and reduced in number with aberrant mitochondria in contrast to the wild type plant [19]
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