2016
DOI: 10.1007/s12275-016-6272-8
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GPH1 is involved in glycerol accumulation in the three-dimensional networks of the nematode-trapping fungus Arthrobotrys oligospora

Abstract: Turgor is very important for the invasive growth of fungal pathogens. Glycerol, a highly osmotic solvent, is considered to play an important role in turgor generation. The nematophagous fungus Arthrobotrys oligospora mainly lives as a saprophyte. In the presence of nematodes, A. oligospora enters the parasitic stage by forming three-dimensional networks (traps) to capture nematodes. In A. oligospora, we found that glycerol accumulated during nematode-induced trap formation. We demonstrated that deleting gph1, … Show more

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Cited by 7 publications
(2 citation statements)
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“…For example, a recent work has generated a strain lacking the signaling scaffold protein Soft and shown that cell-cell fusion is required for ring closure in Duddingtonia flagrans (41). In A. oligospora , ATCC24927-background trapping-deficient mutants have been isolated: adhesin protein Mad1 (42), autophagy protein Atg8 (43), mitogen-activated protein kinase Slt2 (44), pH sensor PalH (45), NADPH oxidase NoxA (46), low-affinity calcium uptake system proteins Fig1 and Fig2 (47), Rab GTPase Rab7A (48), actin-associated protein Crn1 (49), Woronin body component Hex1 (50), malate synthase Mls (51), glycogen phosphorylase Gph1 (52), transcription factors VelB (53) and StuA (54), and microRNA processing protein Qde2 (55), to which we add the G-protein β subunit Gpb1. However, a mechanistic view of how these and other molecular players are interconnected during the interaction of A. oligospora with their prey is totally lacking.…”
Section: Resultsmentioning
confidence: 99%
“…For example, a recent work has generated a strain lacking the signaling scaffold protein Soft and shown that cell-cell fusion is required for ring closure in Duddingtonia flagrans (41). In A. oligospora , ATCC24927-background trapping-deficient mutants have been isolated: adhesin protein Mad1 (42), autophagy protein Atg8 (43), mitogen-activated protein kinase Slt2 (44), pH sensor PalH (45), NADPH oxidase NoxA (46), low-affinity calcium uptake system proteins Fig1 and Fig2 (47), Rab GTPase Rab7A (48), actin-associated protein Crn1 (49), Woronin body component Hex1 (50), malate synthase Mls (51), glycogen phosphorylase Gph1 (52), transcription factors VelB (53) and StuA (54), and microRNA processing protein Qde2 (55), to which we add the G-protein β subunit Gpb1. However, a mechanistic view of how these and other molecular players are interconnected during the interaction of A. oligospora with their prey is totally lacking.…”
Section: Resultsmentioning
confidence: 99%
“…In addition, mutations in latg13 , atg1 , atg4 , and atg5 led to the loss of ability for trap formation in A. oligospora [ 77 , 78 , 79 , 80 ]. Besides autophagy, some cellular processes affect the formation of traps in A. oligospora , such as woronin body synthesis [ 81 ], RNA interference [ 82 ], glycerol biosynthesis [ 83 ], production of reactive oxygen species [ 84 ], F-box protein synthesis [ 85 ], nitrate assimilation pathway [ 86 ], pH-sensing receptor protein synthesis [ 87 ], velvet family protein synthesis [ 88 ], scaffold protein synthesis [ 89 ], lectin synthesis [ 90 ], actin synthesis [ 91 ], and malate synthase [ 92 ]. Finally, research confirms that A. oligospora possesses pathways related to the biosynthesis of SECs of the gene cluster AOL_s00215g, containing 11 genes.…”
Section: Mechanisms Of Trap Formation In a Oligosporamentioning
confidence: 99%