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Article ; Online: Phosphorylation of endogenous α-synuclein induced by extracellular seeds initiates at the pre-synaptic region and spreads to the cell body.

Awa, Shiori / Suzuki, Genjiro / Masuda-Suzukake, Masami / Nonaka, Takashi / Saito, Minoru / Hasegawa, Masato

2022 Volume 12, Issue 1, Page(s) 1163

Abstract: Accumulation of phosphorylated α-synuclein aggregates has been implicated in several diseases, such as Parkinson's disease (PD) and dementia with Lewy bodies (DLB), and is thought to spread in a prion-like manner. Elucidating the mechanisms of prion-like ...

Abstract	Accumulation of phosphorylated α-synuclein aggregates has been implicated in several diseases, such as Parkinson's disease (PD) and dementia with Lewy bodies (DLB), and is thought to spread in a prion-like manner. Elucidating the mechanisms of prion-like transmission of α-synuclein is important for the development of therapies for these diseases, but little is known about the details. Here, we injected α-synuclein fibrils into the brains of wild-type mice and examined the early phase of the induction of phosphorylated α-synuclein accumulation. We found that phosphorylated α-synuclein appeared within a few days after the intracerebral injection. It was observed initially in presynaptic regions and subsequently extended its localization to axons and cell bodies.　These results suggest that extracellular α-synuclein fibrils are taken up into the presynaptic region and seed-dependently convert the endogenous normal α-synuclein that is abundant there to an abnormal phosphorylated form, which is then transported through the axon to the cell body.
MeSH term(s)	Animals ; Axons/metabolism ; Cells, Cultured ; Cerebral Cortex/cytology ; Disease Models, Animal ; Embryo, Mammalian ; Hippocampus/pathology ; Humans ; Male ; Mice ; Neurodegenerative Diseases/pathology ; Phosphorylation ; Primary Cell Culture ; Recombinant Proteins/administration & dosage ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Synapses/metabolism ; Synapses/pathology ; alpha-Synuclein/administration & dosage ; alpha-Synuclein/genetics ; alpha-Synuclein/isolation & purification ; alpha-Synuclein/metabolism
Chemical Substances	Recombinant Proteins ; Snca protein, mouse ; alpha-Synuclein
Language	English
Publishing date	2022-01-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-04780-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Following the fate of endocytosed fibrils.

Hasegawa, Masato / Suzuki, Genjiro

The Journal of biological chemistry

2017 Volume 292, Issue 32, Page(s) 13498–13499

Abstract: Cell-to-cell transmission of intracellular protein aggregates is considered a central event in many neurodegenerative diseases, but little is known about the underlying molecular mechanisms. A new study employs fluorescence quenching to examine the fate ... ...

Abstract	Cell-to-cell transmission of intracellular protein aggregates is considered a central event in many neurodegenerative diseases, but little is known about the underlying molecular mechanisms. A new study employs fluorescence quenching to examine the fate of α-synuclein, a key molecule in the pathology of Parkinson's disease and related disorders, in primary cultured neurons, finding that endocytosis and lysosomal processing of exogenous fibrils may explain the transmission of α-synuclein pathology.
MeSH term(s)	Animals ; Endocytosis ; Humans ; Lysosomes/metabolism ; Lysosomes/pathology ; Lysosomes/ultrastructure ; Models, Biological ; Neurons/metabolism ; Neurons/pathology ; Neurons/ultrastructure ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; alpha-Synuclein/chemistry ; alpha-Synuclein/metabolism
Chemical Substances	SNCA protein, human ; alpha-Synuclein
Language	English
Publishing date	2017-08-10
Publishing country	United States
Document type	Editorial ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.H117.780296
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Article ; Online: Dysregulation of the progranulin-driven autophagy-lysosomal pathway mediates secretion of the nuclear protein TDP-43.

Tanaka, Yoshinori / Ito, Shun-Ichi / Honma, Yuki / Hasegawa, Masato / Kametani, Fuyuki / Suzuki, Genjiro / Kozuma, Lina / Takeya, Kosuke / Eto, Masumi

The Journal of biological chemistry

2023 Volume 299, Issue 11, Page(s) 105272

Abstract: The cytoplasmic accumulation of the nuclear protein transactive response DNA-binding protein 43 kDa (TDP-43) has been linked to the progression of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 secreted into the extracellular ...

Abstract	The cytoplasmic accumulation of the nuclear protein transactive response DNA-binding protein 43 kDa (TDP-43) has been linked to the progression of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 secreted into the extracellular space has been suggested to contribute to the cell-to-cell spread of the cytoplasmic accumulation of TDP-43 throughout the brain; however, the underlying mechanisms remain unknown. We herein demonstrated that the secretion of TDP-43 was stimulated by the inhibition of the autophagy-lysosomal pathway driven by progranulin (PGRN), a causal protein of frontotemporal lobar degeneration. Among modulators of autophagy, only vacuolar-ATPase inhibitors, such as bafilomycin A1 (Baf), increased the levels of the full-length and cleaved forms of TDP-43 and the autophagosome marker LC3-II (microtubule-associated proteins 1A/1B light chain 3B) in extracellular vesicle fractions prepared from the culture media of HeLa, SH-SY5Y, or NSC-34 cells, whereas vacuolin-1, MG132, chloroquine, rapamycin, and serum starvation did not. The C-terminal fragment of TDP-43 was required for Baf-induced TDP-43 secretion. The Baf treatment induced the translocation of the aggregate-prone GFP-tagged C-terminal fragment of TDP-43 and mCherry-tagged LC3 to the plasma membrane. The Baf-induced secretion of TDP-43 was attenuated in autophagy-deficient ATG16L1 knockout HeLa cells. The knockdown of PGRN induced the secretion of cleaved TDP-43 in an autophagy-dependent manner in HeLa cells. The KO of PGRN in mouse embryonic fibroblasts increased the secretion of the cleaved forms of TDP-43 and LC3-II. The treatment inducing TDP-43 secretion increased the nuclear translocation of GFP-tagged transcription factor EB, a master regulator of the autophagy-lysosomal pathway in SH-SY5Y cells. These results suggest that the secretion of TDP-43 is promoted by dysregulation of the PGRN-driven autophagy-lysosomal pathway.
MeSH term(s)	Humans ; Autophagy/drug effects ; Autophagy/genetics ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; HeLa Cells ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Lysosomes/metabolism ; Progranulins/genetics ; Progranulins/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Gene Expression Regulation/drug effects ; Extracellular Vesicles/metabolism ; Enzyme Inhibitors/pharmacology ; Autophagosomes/drug effects ; Autophagosomes/metabolism ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism
Chemical Substances	DNA-Binding Proteins ; Intercellular Signaling Peptides and Proteins ; Progranulins ; TDP-43 protein, mouse ; benzyloxycarbonylleucyl-leucyl-leucine aldehyde (RF1P63GW3K) ; bafilomycin A1 (88899-55-2) ; MAP1LC3B protein, human ; Microtubule-Associated Proteins ; Enzyme Inhibitors ; ATG16L1 protein, human ; Autophagy-Related Proteins
Language	English
Publishing date	2023-09-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105272
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Article: [The proceeding of drug development based on the propagation of tau protein].

Suzuki, Genjiro / Hasegawa, Masato

Nihon rinsho. Japanese journal of clinical medicine

2016 Volume 74, Issue 3, Page(s) 432–437

Abstract: Many neurodegenerative diseases accompanied by dementia are associated with the accumulation of protein aggregates. These aggregates are thought to be causes of progressive neurodegeneration and death of neurons. Recent studies indicated that these ... ...

Abstract	Many neurodegenerative diseases accompanied by dementia are associated with the accumulation of protein aggregates. These aggregates are thought to be causes of progressive neurodegeneration and death of neurons. Recent studies indicated that these aggregates could propagate between cells in a prion like manner. Once a protein aggregate is formed it can transmit cell to cell and affect broad regions of brain. Some neurodegenerative diseases such as Alzheimer's disease are associated with the pathological aggregation of tau protein. Thus, these diseases are named as tauopathies. In the brain of these diseases, aggregated tau must also propagate in a prion like manner. Here, we discuss about the therapeutic approaches against dementia based on the prion like propagation of tau proteins.
MeSH term(s)	Alternative Splicing ; Drug Design ; Exons ; Humans ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Tauopathies/drug therapy ; Tauopathies/genetics ; Tauopathies/metabolism ; tau Proteins/chemistry ; tau Proteins/metabolism
Chemical Substances	Protein Isoforms ; tau Proteins
Language	Japanese
Publishing date	2016-03
Publishing country	Japan
Document type	English Abstract ; Journal Article
ZDB-ID	390903-7
ISSN	0047-1852
ISSN	0047-1852
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Article ; Online: Dextran sulphate-induced tau assemblies cause endogenous tau aggregation and propagation in wild-type mice.

Masuda-Suzukake, Masami / Suzuki, Genjiro / Hosokawa, Masato / Nonaka, Takashi / Goedert, Michel / Hasegawa, Masato

Brain communications

2020 Volume 2, Issue 2, Page(s) fcaa091

Abstract: Accumulation of assembled tau protein in the central nervous system is characteristic of Alzheimer's disease and several other neurodegenerative diseases, called tauopathies. Recent studies have revealed that propagation of assembled tau is key to ... ...

Abstract	Accumulation of assembled tau protein in the central nervous system is characteristic of Alzheimer's disease and several other neurodegenerative diseases, called tauopathies. Recent studies have revealed that propagation of assembled tau is key to understanding the pathological mechanisms of these diseases. Mouse models of tau propagation are established by injecting human-derived tau seeds intracerebrally; nevertheless, these have a limitation in terms of regulation of availability. To date, no study has shown that synthetic assembled tau induce tau propagation in non-transgenic mice. Here we confirm that dextran sulphate, a sulphated glycosaminoglycan, induces the assembly of recombinant tau protein into filaments
Language	English
Publishing date	2020-07-08
Publishing country	England
Document type	Journal Article
ISSN	2632-1297
ISSN (online)	2632-1297
DOI	10.1093/braincomms/fcaa091
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Article ; Online: Active conversion to the prion state as a molecular switch for cellular adaptation to environmental stress.

Suzuki, Genjiro / Tanaka, Motomasa

BioEssays : news and reviews in molecular, cellular and developmental biology

2013 Volume 35, Issue 1, Page(s) 12–16

MeSH term(s)	Adaptation, Physiological ; Alkyl and Aryl Transferases/chemistry ; Alkyl and Aryl Transferases/metabolism ; Humans ; Podospora/metabolism ; PrPC Proteins/chemistry ; PrPC Proteins/metabolism ; Prions ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Stress, Physiological
Chemical Substances	PrPC Proteins ; Prions ; Saccharomyces cerevisiae Proteins ; Alkyl and Aryl Transferases (EC 2.5.-) ; MOD5 protein, S cerevisiae (EC 2.5.1.75)
Language	English
Publishing date	2013-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.201200121
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Article ; Online: Expanding the yeast prion world: Active prion conversion of non-glutamine/asparagine-rich Mod5 for cell survival.

Suzuki, Genjiro / Tanaka, Motomasa

Prion

2012 Volume 7, Issue 2, Page(s) 109–113

Abstract: Mammalian and fungal prion proteins form self-perpetuating β-sheet-rich fibrillar aggregates called amyloid. Prion inheritance is based on propagation of the regularly oriented amyloid structures of the prion proteins. All yeast prion proteins identified ...

Abstract	Mammalian and fungal prion proteins form self-perpetuating β-sheet-rich fibrillar aggregates called amyloid. Prion inheritance is based on propagation of the regularly oriented amyloid structures of the prion proteins. All yeast prion proteins identified thus far contain aggregation-prone glutamine/asparagine (Gln/Asn)-rich domains, although the mammalian prion protein and fungal prion protein HET-s do not contain such sequences. In order to fill this gap, we searched for novel yeast prion proteins lacking Gln/Asn-rich domains via a genome-wide screen based on cross-seeding between two heterologous proteins and identified Mod5, a yeast tRNA isopentenyltransferase, as a novel non-Gln/Asn-rich yeast prion protein. Mod5 formed self-propagating amyloid fibers in vitro and the introduction of Mod5 amyloids into non-prion yeast induced dominantly and cytoplasmically heritable prion state [MOD (+) ], which harbors aggregates of endogenous Mod5. [MOD (+) ] yeast showed an increased level of membrane lipid ergosterol and acquired resistance to antifungal agents. Importantly, enhanced de novo formation of [MOD (+) ] was observed when non-prion yeast was grown under selective pressures from antifungal drugs. Our findings expand the family of yeast prions to non-Gln/Asn-rich proteins and reveal the acquisition of a fitness advantage for cell survival through active prion conversion.
MeSH term(s)	Alkyl and Aryl Transferases/metabolism ; Amyloid/metabolism ; Antifungal Agents/pharmacology ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Genome, Fungal ; Microbial Viability ; Prions/genetics ; Prions/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Stress, Physiological/physiology ; Yeasts/genetics ; Yeasts/metabolism
Chemical Substances	Amyloid ; Antifungal Agents ; Fungal Proteins ; Prions ; Saccharomyces cerevisiae Proteins ; Alkyl and Aryl Transferases (EC 2.5.-) ; MOD5 protein, S cerevisiae (EC 2.5.1.75) ; tRNA isopentenyltransferase (EC 2.5.1.75)
Language	English
Publishing date	2012-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267671-5
ISSN	1933-690X ; 1933-690X
ISSN (online)	1933-690X
ISSN	1933-690X
DOI	10.4161/pri.22685
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Article ; Online: [KIL-d] Protein Element Confers Antiviral Activity via Catastrophic Viral Mutagenesis.

Suzuki, Genjiro / Weissman, Jonathan S / Tanaka, Motomasa

Molecular cell

2015 Volume 60, Issue 4, Page(s) 651–660

Abstract: Eukaryotic cells are targeted by pathogenic viruses and have developed cell defense mechanisms against viral infection. In yeast, the cellular extrachromosomal genetic element [KIL-d] alters killer activity of M double-stranded RNA killer virus and ... ...

Abstract	Eukaryotic cells are targeted by pathogenic viruses and have developed cell defense mechanisms against viral infection. In yeast, the cellular extrachromosomal genetic element [KIL-d] alters killer activity of M double-stranded RNA killer virus and confers cell resistance against the killer virus. However, its underlying mechanism and the molecular nature of [KIL-d] are unknown. Here, we demonstrate that [KIL-d] is a proteinaceous prion-like aggregate with non-Mendelian cytoplasmic transmission. Deep sequencing analyses revealed that [KIL-d] selectively increases the rate of de novo mutation in the killer toxin gene of the viral genome, producing yeast harboring a defective mutant killer virus with a selective growth advantage over those with WT killer virus. These results suggest that a prion-like [KIL-d] element reprograms the viral replication machinery to induce mutagenesis and genomic inactivation via the long-hypothesized mechanism of "error catastrophe." The findings also support a role for prion-like protein aggregates in cellular defense and adaptation.
MeSH term(s)	Antiviral Agents/metabolism ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Gene Expression Regulation, Viral ; High-Throughput Nucleotide Sequencing ; Mutation ; RNA, Double-Stranded/metabolism ; RNA, Viral/metabolism ; Sequence Analysis, DNA ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication
Chemical Substances	Antiviral Agents ; Fungal Proteins ; RNA, Double-Stranded ; RNA, Viral ; Viral Proteins
Language	English
Publishing date	2015-11-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2015.10.020
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Article: [KIL-d] Protein Element Confers Antiviral Activity via Catastrophic Viral Mutagenesis

Suzuki, Genjiro / JonathanÂ S. Weissman / Motomasa Tanaka

Molecular cell. 2015 Nov. 19, v. 60

2015

Abstract	Eukaryotic cells are targeted by pathogenic viruses and have developed cell defense mechanisms against viral infection. In yeast, the cellular extrachromosomal genetic element [KIL-d] alters killer activity of M double-stranded RNA killer virus and confers cell resistance against the killer virus. However, its underlying mechanism and the molecular nature of [KIL-d] are unknown. Here, we demonstrate that [KIL-d] is a proteinaceous prion-like aggregate with non-Mendelian cytoplasmic transmission. Deep sequencing analyses revealed that [KIL-d] selectively increases the rate of de novo mutation in the killer toxin gene of the viral genome, producing yeast harboring a defective mutant killer virus with a selective growth advantage over those with WT killer virus. These results suggest that a prion-like [KIL-d] element reprograms the viral replication machinery to induce mutagenesis and genomic inactivation via the long-hypothesized mechanism of âerror catastrophe.â The findings also support a role for prion-like protein aggregates in cellular defense and adaptation.
Keywords	antiviral properties ; defense mechanisms ; double-stranded RNA ; eukaryotic cells ; genes ; high-throughput nucleotide sequencing ; mutagenesis ; mutants ; protein aggregates ; virus replication ; viruses ; yeasts
Language	English
Dates of publication	2015-1119
Size	p. 651-660.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2015.10.020
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: α-synuclein strains that cause distinct pathologies differentially inhibit proteasome.

Suzuki, Genjiro / Imura, Sei / Hosokawa, Masato / Katsumata, Ryu / Nonaka, Takashi / Hisanaga, Shin-Ichi / Saeki, Yasushi / Hasegawa, Masato

eLife

2020 Volume 9

Abstract: Abnormal α-synuclein aggregation has been implicated in several diseases and is known to spread in a prion-like manner. There is a relationship between protein aggregate structure (strain) and clinical phenotype in prion diseases, however, whether ... ...

Abstract	Abnormal α-synuclein aggregation has been implicated in several diseases and is known to spread in a prion-like manner. There is a relationship between protein aggregate structure (strain) and clinical phenotype in prion diseases, however, whether differences in the strains of α-synuclein aggregates account for the different pathologies remained unclear. Here, we generated two types of α-synuclein fibrils from identical monomer and investigated their seeding and propagation ability in mice and primary-cultured neurons. One α-synuclein fibril induced marked accumulation of phosphorylated α-synuclein and ubiquitinated protein aggregates, while the other did not, indicating the formation of α-synuclein two strains. Notably, the former α-synuclein strain inhibited proteasome activity and co-precipitated with 26S proteasome complex. Further examination indicated that structural differences in the C-terminal region of α-synuclein strains lead to different effects on proteasome activity. These results provide a possible molecular mechanism to account for the different pathologies induced by different α-synuclein strains.
MeSH term(s)	Animals ; Cells, Cultured ; Fungal Proteins/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Neurons/pathology ; Proteasome Endopeptidase Complex/metabolism ; Saccharomyces cerevisiae/chemistry ; alpha-Synuclein/metabolism
Chemical Substances	Fungal Proteins ; alpha-Synuclein ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATP dependent 26S protease (EC 3.4.99.-)
Language	English
Publishing date	2020-07-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.56825
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