Endocytosis of a maltose permease is induced when amylolytic enzyme production is repressed in Aspergillus oryzae

Hiramoto, Tetsuya; Tanaka, Mizuki; Ichikawa, Takanori; Matsuura, Yuka; Hasegawa-Shiro, Sachiko; Shintani, Takahiro; Gomi, Katsuya

doi:10.1016/j.fgb.2015.05.015

Cited by 26 publications

(21 citation statements)

References 44 publications

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“…The majority of the GFP fluorescence disappeared from the plasma membrane of the wild-type strain after 30 min of incubation in the glucose-containing medium; however, strong GFP fluorescence was observed in the intracellular compartments that were presumed to be vacuoles (Fig. 1C) in accordance with our previous study (5). In contrast, GFP fluorescence was observed at the plasma membrane of the ΔcreD mutant even after 120 min of incubation in the glucose-containing medium (Fig.…”

supporting

confidence: 90%

“…In a previous paper, we showed that MalP endocytosis was rapidly induced by CCR-inducing sugars, whereas repression of HulA expression inhibited this endocytosis (5). In this study, we demonstrated that HulA interacts with the arrestin-like protein CreD and that CreD is required for both MalP endocytosis and CCR relief.…”

Section: Discussionsupporting

confidence: 52%

“…Fluorescence imaging of GFP-MalP with a confocal fluorescence microscope was performed as described previously (5).…”

Section: Methodsmentioning

confidence: 99%

“…CreA-mediated CCR and rapid endocytosis of MalP were induced by glucose and mannose, but not by maltose and xylose (5). To examine the effects of these sugars on the phosphorylation state of CreD, the CreD-3ϫFLAG- Improved ␣-Amylase Production by CreD Mutant Applied and Environmental Microbiology expressing strain was incubated in minimal medium (MM) containing these sugars.…”

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confidence: 99%

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Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillusoryzae

Tanaka

Hiramoto

Tada

et al. 2017

Appl Environ Microbiol

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Aspergillus oryzae produces copious amount of amylolytic enzymes, and MalP, a major maltose permease, is required for the expression of amylase-encoding genes. The expression of these genes is strongly repressed by carbon catabolite repression (CCR) in the presence of glucose. MalP is transported from the plasma membrane to the vacuole by endocytosis, which requires the homolog of E6-AP carboxyl terminus ubiquitin ligase HulA, an ortholog of yeast Rsp5. In yeast, arrestin-like proteins mediate endocytosis as adaptors of Rsp5 and transporters. In the present study, we examined the involvement of CreD, an arrestin-like protein, in glucoseinduced MalP endocytosis and CCR of amylase-encoding genes. Deletion of creD inhibited the glucose-induced endocytosis of MalP, and CreD showed physical interaction with HulA. Phosphorylation of CreD was detected by Western blotting, and two serine residues were determined as the putative phosphorylation sites. However, the phosphorylation state of the serine residues did not regulate MalP endocytosis and its interaction with HulA. Although ␣-amylase production was significantly repressed by creD deletion, both phosphorylation and dephosphorylation mimics of CreD had a negligible effect on ␣-amylase activity. Interestingly, dephosphorylation of CreD was required for CCR relief of amylase genes that was triggered by disruption of the deubiquitinating enzyme-encoding gene creB. The ␣-amylase activity of the creB mutant was 1.6-fold higher than that of the wild type, and the dephosphorylation mimic of CreD further improved the ␣-amylase activity by 2.6-fold. These results indicate that a combination of the dephosphorylation mutation of CreD and creB disruption increased the production of amylolytic enzymes in A. oryzae. IMPORTANCEIn eukaryotes, glucose induces carbon catabolite repression (CCR) and proteolytic degradation of plasma membrane transporters via endocytosis. Glucoseinduced endocytosis of transporters is mediated by their ubiquitination, and arrestinlike proteins act as adaptors of transporters and ubiquitin ligases. In this study, we showed that CreD, an arrestin-like protein, is involved in glucose-induced endocytosis of maltose permease and carbon catabolite derepression of amylase gene expression in Aspergillus oryzae. Dephosphorylation of CreD was required for CCR relief triggered by the disruption of creB, which encodes a deubiquitinating enzyme; a combination of the phosphorylation-defective mutation of CreD and creB disruption dramatically improved ␣-amylase production. This study shows the dual function of an arrestin-like protein and provides a novel approach for improving the production of amylolytic enzymes in A. oryzae.

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supporting

confidence: 90%

Section: Discussionsupporting

confidence: 52%

“…Fluorescence imaging of GFP-MalP with a confocal fluorescence microscope was performed as described previously (5).…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillusoryzae

Tanaka

Hiramoto

Tada

et al. 2017

Appl Environ Microbiol

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“…In addition to amylolytic gene induction by maltose, xylose induces xylanolytic and cellulolytic gene expression in A. oryzae (Noguchi et al, ). Although 1 mM xylose can function as a repressing carbon source in Aspergillus niger (de Vries et al ), 1% xylose had no apparent effect on amylase production in A. oryzae (Hiramoto et al ). In contrast, 1% mannose strongly inhibited amylase production as with glucose (Hiramoto et al ).…”

Section: Resultsmentioning

confidence: 99%

Nuclear export‐dependent degradation of the carbon catabolite repressor CreA is regulated by a region located near the C‐terminus in Aspergillus oryzae

Tanaka

Ichinose

Shintani

et al. 2018

Molecular Microbiology

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Carbon catabolite repression (CCR) is regulated by the C H -type transcription factor CreA/Cre1 in filamentous fungi including Aspergillus oryzae. We investigated the stability and subcellular localization of CreA in A. oryzae. The abundance of FLAG-tagged CreA (FLAG-CreA) was dramatically reduced after incubation in maltose and xylose, which stimulated the export of CreA from the nucleus to the cytoplasm. Mutation of a putative nuclear export signal resulted in nuclear retention and significant stabilization of CreA. These results suggest that CreA is rapidly degraded in the cytoplasm after export from the nucleus. The FLAG-CreA protein level was reduced by disruption of creB and creC, which encode the deubiquitinating enzyme complex involved in CCR. In contrast, FLAG-CreA stability was not affected by disruption of creD which encodes an arrestin-like protein required for CCR relief. Deletion of the last 40 C-terminal amino acids resulted in remarkable stabilization and increased abundance of FLAG-CreA, whereas deletion of the last 20 C-terminal amino acids had no apparent effect on CreA stability. This result suggests that the 20 amino acid region located between positions 390 and 409 of CreA is critical for the rapid degradation of CreA.

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CreA-independent carbon catabolite repression of cellulase genes by trimeric G-protein and protein kinase A in Aspergillus nidulans

Kunitake

Uchida

et al. 2019

Curr Genet

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Endocytosis of a maltose permease is induced when amylolytic enzyme production is repressed in Aspergillus oryzae

Cited by 26 publications

References 44 publications

Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillusoryzae

Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillusoryzae

Nuclear export‐dependent degradation of the carbon catabolite repressor CreA is regulated by a region located near the C‐terminus in Aspergillus oryzae

CreA-independent carbon catabolite repression of cellulase genes by trimeric G-protein and protein kinase A in Aspergillus nidulans

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