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Article ; Online: Foreword.

Nakanishi-Matsui, Mayumi

2022 Volume 45, Issue 10, Page(s) 1403

Language	English
Publishing date	2022-08-18
Publishing country	Japan
Document type	Journal Article
ZDB-ID	1150271-x
ISSN	1347-5215 ; 0918-6158
ISSN (online)	1347-5215
ISSN	0918-6158
DOI	10.1248/bpb.b22-ctf4510
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Article ; Online: V-ATPase a3 Subunit in Secretory Lysosome Trafficking in Osteoclasts.

Nakanishi-Matsui, Mayumi / Matsumoto, Naomi

Biological & pharmaceutical bulletin

2022 Volume 45, Issue 10, Page(s) 1426–1431

Abstract: Vacuolar-type ATPase (V-ATPase) shares its structure and rotational catalysis with F-type ATPase (F-ATPase, ATP synthase). However, unlike subunits of F-ATPase, those of V-ATPase have tissue- and/or organelle-specific isoforms. Structural diversity of V- ... ...

Abstract	Vacuolar-type ATPase (V-ATPase) shares its structure and rotational catalysis with F-type ATPase (F-ATPase, ATP synthase). However, unlike subunits of F-ATPase, those of V-ATPase have tissue- and/or organelle-specific isoforms. Structural diversity of V-ATPase generated by different combinations of subunit isoforms enables it to play diverse physiological roles in mammalian cells. Among these various roles, this review focuses on the functions of lysosome-specific V-ATPase in bone resorption by osteoclasts. Lysosomes remain in the cytoplasm in most cell types, but in osteoclasts, secretory lysosomes move toward and fuse with the plasma membrane to secrete lysosomal enzymes, which is essential for bone resorption. Through this process, lysosomal V-ATPase harboring the a3 isoform of the a subunit is relocated to the plasma membrane, where it transports protons from the cytosol to the cell exterior to generate the acidic extracellular conditions required for secreted lysosomal enzymes. In addition to this role as a proton pump, we recently found that the lysosomal a3 subunit of V-ATPase is essential for anterograde trafficking of secretory lysosomes. Specifically, a3 interacts with Rab7, a member of the Rab guanosine 5'-triphosphatase (GTPase) family that regulates organelle trafficking, and recruits it to the lysosomal membrane. These findings revealed the multifunctionality of lysosomal V-ATPase in osteoclasts; V-ATPase is responsible not only for the formation of the acidic environment by transporting protons, but also for intracellular trafficking of secretory lysosomes by recruiting organelle trafficking factors. Herein, we summarize the molecular mechanism underlying secretory lysosome trafficking in osteoclasts, and discuss the possible regulatory role of V-ATPase in organelle trafficking.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Animals ; Bone Resorption/metabolism ; GTP Phosphohydrolases/metabolism ; Guanosine/metabolism ; Humans ; Lysosomes/metabolism ; Mammals/metabolism ; Osteoclasts/metabolism ; Protein Isoforms/metabolism ; Protons ; Vacuolar Proton-Translocating ATPases/metabolism
Chemical Substances	Protein Isoforms ; Protons ; Guanosine (12133JR80S) ; Adenosine Triphosphate (8L70Q75FXE) ; GTP Phosphohydrolases (EC 3.6.1.-) ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-)
Language	English
Publishing date	2022-08-17
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	1150271-x
ISSN	1347-5215 ; 0918-6158
ISSN (online)	1347-5215
ISSN	0918-6158
DOI	10.1248/bpb.b22-00371
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Article ; Online: Role of the Cytosolic Domain of the a3 Subunit of V-ATPase in the Interaction with Rab7 and Secretory Lysosome Trafficking in Osteoclasts.

Nakanishi-Matsui, Mayumi / Matsumoto, Naomi / Sun-Wada, Ge-Hong / Wada, Yoh

Biological & pharmaceutical bulletin

2024 Volume 47, Issue 1, Page(s) 339–344

Abstract: We previously reported that the a3 subunit of proton-pumping vacuolar-type ATPase (V-ATPase) interacts with Rab7 and its guanine nucleotide exchange factor, Mon1a-Ccz1, and recruits them to secretory lysosomes in osteoclasts, which is essential for ... ...

Abstract	We previously reported that the a3 subunit of proton-pumping vacuolar-type ATPase (V-ATPase) interacts with Rab7 and its guanine nucleotide exchange factor, Mon1a-Ccz1, and recruits them to secretory lysosomes in osteoclasts, which is essential for anterograde trafficking of secretory lysosomes. The a3 subunit interacts with Mon1a-Ccz1 through its cytosolic N-terminal domain. Here, we examined the roles of this domain in the interaction with Rab7 and trafficking of secretory lysosomes. Immunoprecipitation experiments showed that a3 interacted with Rab7 through its cytosolic domain, similar to the interaction with Mon1a-Ccz1. We connected this domain with a lysosome localization signal and expressed it in a3-knockout (a3KO) osteoclasts. Although the signal connected to the cytosolic domain was mainly detected in lysosomes, impaired lysosome trafficking in a3KO osteoclasts was not rescued. These results indicate that the cytosolic domain of a3 can interact with trafficking regulators, but is insufficient to induce secretory lysosome trafficking. The C-terminal domain of a3 and other subunits of V-ATPase are likely required to form a fully functional complex for secretory lysosome trafficking.
MeSH term(s)	Biological Transport ; Lysosomes/metabolism ; Osteoclasts/metabolism ; Vacuolar Proton-Translocating ATPases/metabolism ; Animals ; Mice ; rab7 GTP-Binding Proteins/chemistry ; rab7 GTP-Binding Proteins/metabolism
Chemical Substances	Vacuolar Proton-Translocating ATPases (EC 3.6.1.-) ; rab7 GTP-binding proteins, mouse ; rab7 GTP-Binding Proteins
Language	English
Publishing date	2024-01-31
Publishing country	Japan
Document type	Journal Article
ZDB-ID	1150271-x
ISSN	1347-5215 ; 0918-6158
ISSN (online)	1347-5215
ISSN	0918-6158
DOI	10.1248/bpb.b23-00833
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Article ; Online: Proton pumping V-ATPase inhibitor bafilomycin A1 affects Rab7 lysosomal localization and abolishes anterograde trafficking of osteoclast secretory lysosomes.

Matsumoto, Naomi / Nakanishi-Matsui, Mayumi

Biochemical and biophysical research communications

2019 Volume 510, Issue 3, Page(s) 421–426

Abstract: Osteoclast lysosomes secrete lytic enzymes into bone resorption lacunae, and sort the lysosomal proton pumping vacuolar-type ATPase (V-ATPase) to the plasma membrane to form the acidic environment required for bone digestion. The a3 isoform of V-ATPase ... ...

Abstract	Osteoclast lysosomes secrete lytic enzymes into bone resorption lacunae, and sort the lysosomal proton pumping vacuolar-type ATPase (V-ATPase) to the plasma membrane to form the acidic environment required for bone digestion. The a3 isoform of V-ATPase is essential for outward trafficking of the secretory lysosomes and interacts physically with Rab7, a small GTPase that regulates trafficking of late endosomes and lysosomes, to recruit it to lysosomes. However, it is unclear whether organelle acidification by V-ATPase is required for the lysosome trafficking. Here, we showed that incubation of osteoclasts with the V-ATPase inhibitor bafilomycin A1 abolished the osteoclast-characteristic peripheral localization of secretory lysosomes, Rab7, and α-tubulin. Although bafilomycin A1 had little or no effect on Rab7 activation and its interaction with a3, treatment with the inhibitor significantly reduced the lysosomal localization of Rab7. Even constitutively active Rab7 did not localize to lysosomes in the presence of the inhibitor. These results suggest that organelle acidification by V-ATPase is required for localization of activated Rab7 to lysosomes.
MeSH term(s)	Animals ; Biological Transport/drug effects ; Enzyme Inhibitors/pharmacology ; HEK293 Cells ; Humans ; Lysosomes/chemistry ; Lysosomes/drug effects ; Macrolides/pharmacology ; Mice, Inbred C57BL ; Osteoclasts/chemistry ; Osteoclasts/drug effects ; Tubulin/analysis ; Vacuolar Proton-Translocating ATPases/antagonists & inhibitors ; rab GTP-Binding Proteins/analysis
Chemical Substances	Enzyme Inhibitors ; Macrolides ; Tubulin ; rab7 protein (152989-05-4) ; bafilomycin A1 (88899-55-2) ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2019-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2019.01.118
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Article ; Online: The lysosomal V-ATPase a3 subunit is involved in localization of Mon1-Ccz1, the GEF for Rab7, to secretory lysosomes in osteoclasts.

Matsumoto, Naomi / Sekiya, Mizuki / Sun-Wada, Ge-Hong / Wada, Yoh / Nakanishi-Matsui, Mayumi

Scientific reports

2022 Volume 12, Issue 1, Page(s) 8455

Abstract: We have shown previously that the lysosomal a3 isoform of the a subunit of vacuolar-type ATPase (V-ATPase) interacts with inactive (GDP-bound form) Rab7, a small GTPase that regulates late endosome/lysosome trafficking, and that a3 recruits Rab7 to ... ...

Abstract	We have shown previously that the lysosomal a3 isoform of the a subunit of vacuolar-type ATPase (V-ATPase) interacts with inactive (GDP-bound form) Rab7, a small GTPase that regulates late endosome/lysosome trafficking, and that a3 recruits Rab7 to secretory lysosomes in mouse osteoclasts. This is essential for outward trafficking of secretory lysosomes and thus for bone resorption. However, the molecular mechanism underlying the recruitment of Rab7 by a3 remains to be fully elucidated. Here, we showed that a3 interacts with the Mon1A-Ccz1 complex, a guanine nucleotide exchange factor (GEF) for Rab7, using HEK293T cells. The interaction was mediated by the amino-terminal half domain of a3 and the longin motifs of Mon1A and Ccz1. Exogenous expression of the GEF promoted the interaction between a3 and Rab7. Mon1A mutants that interact inefficiently with Rab7 interacted with a3 at a similar level to wild-type Mon1A. Lysosomal localization of endogenous Ccz1 was abolished in osteoclasts lacking a3. These results suggest that the lysosomal a3 isoform of V-ATPase interacts with Mon1A-Ccz1, and that a3 is important for Mon1A-Ccz1 localization to secretory lysosomes, which mediates Rab7 recruitment to the organelle.
MeSH term(s)	Animals ; Endosomes/metabolism ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; HEK293 Cells ; Humans ; Lysosomes/metabolism ; Mice ; Osteoclasts/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Vacuolar Proton-Translocating ATPases/genetics ; Vacuolar Proton-Translocating ATPases/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Guanine Nucleotide Exchange Factors ; Protein Isoforms ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-05-19
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/s41598-022-12397-w
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Article ; Online: F-type proton-pumping ATPase mediates acid tolerance in Streptococcus mutans.

Sekiya, Mizuki / Ikeda, Kazuya / Yonai, Ayaka / Ishikawa, Taichi / Shimoyama, Yu / Kodama, Yoshitoyo / Sasaki, Minoru / Nakanishi-Matsui, Mayumi

Journal of applied microbiology

2023 Volume 134, Issue 4

Abstract: Aims: Streptococcus mutans is highly sensitive to inhibitors of proton-pumping F-type ATPase (F-ATPase) under acidic conditions. Herein, we investigated the role of S. mutans F-ATPase in acid tolerance using a bacterium expressing the F-ATPase β subunit ...

Abstract	Aims: Streptococcus mutans is highly sensitive to inhibitors of proton-pumping F-type ATPase (F-ATPase) under acidic conditions. Herein, we investigated the role of S. mutans F-ATPase in acid tolerance using a bacterium expressing the F-ATPase β subunit at lower levels than the wild-type strain. Methods and results: We generated a mutant S. mutans expressing the catalytic β subunit of F-ATPase at lower levels than the wild-type bacterium. The mutant cells exhibited a significantly slower growth rate at pH 5.30, whereas the rate was essentially the same as that of wild-type cells at pH 7.40. In addition, the colony-forming ability of the mutant was decreased at pH <4.30 but not at pH 7.40. Thus, the growth rate and survival of S. mutans expressing low levels of the β subunit were reduced under acidic conditions. Conclusions: Together with our previous observations, this study indicates that F-ATPase is involved in the acid tolerance mechanism of S. mutans by secreting protons from the cytoplasm.
MeSH term(s)	Adenosine Triphosphatases/genetics ; Proton Pumps/genetics ; Protons ; Streptococcus mutans ; Hydrogen-Ion Concentration
Chemical Substances	Adenosine Triphosphatases (EC 3.6.1.-) ; Proton Pumps ; Protons
Language	English
Publishing date	2023-03-31
Publishing country	England
Document type	Journal Article
ZDB-ID	1358023-1
ISSN	1365-2672 ; 1364-5072
ISSN (online)	1365-2672
ISSN	1364-5072
DOI	10.1093/jambio/lxad073
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Article: ATP synthase from Escherichia coli: Mechanism of rotational catalysis, and inhibition with the ε subunit and phytopolyphenols

Nakanishi-Matsui, Mayumi / Mizuki Sekiya / Masamitsu Futai

Biochimica et biophysica acta. 2016 Feb., v. 1857, no. 2

2016

Abstract: ATP synthases (FoF1) are found ubiquitously in energy-transducing membranes of bacteria, mitochondria, and chloroplasts. These enzymes couple proton transport and ATP synthesis or hydrolysis through subunit rotation, which has been studied mainly by ... ...

Abstract	ATP synthases (FoF1) are found ubiquitously in energy-transducing membranes of bacteria, mitochondria, and chloroplasts. These enzymes couple proton transport and ATP synthesis or hydrolysis through subunit rotation, which has been studied mainly by observing single molecules.In this review, we discuss the mechanism of rotational catalysis of ATP synthases, mainly that from Escherichia coli, emphasizing the high-speed and stochastic rotation including variable rates and an inhibited state. Single molecule studies combined with structural information of the bovine mitochondrial enzyme and mutational analysis have been informative as to an understanding of the catalytic site and the interaction between rotor and stator subunits. We discuss the similarity and difference in structure and inhibitory regulation of F1 from bovine and E. coli.Unlike the crystal structure of bovine F1 (α3β3γ), that of E. coli contains a ε subunit, which is a known inhibitor of bacterial and chloroplast F1 ATPases. The carboxyl terminal domain of E. coli ε (εCTD) interacts with the catalytic and rotor subunits (β and γ, respectively), and then inhibits rotation. The effects of phytopolyphenols on F1-ATPase are also discussed: one of them, piceatannol, lowered the rotational speed by affecting rotor/stator interactions.
Keywords	Escherichia coli ; H+/K+-exchanging ATPase ; H-transporting ATP synthase ; adenosine triphosphate ; adenosinetriphosphatase ; bacteria ; catalytic activity ; cattle ; chloroplasts ; crystal structure ; energy metabolism ; hydrolysis ; mitochondria ; mutational analysis
Language	English
Dates of publication	2016-02
Size	p. 129-140.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2015.11.005
Database	NAL-Catalogue (AGRICOLA)

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Article: ATP synthase from Escherichia coli: Mechanism of rotational catalysis, and inhibition with the ε subunit and phytopolyphenols.

Nakanishi-Matsui, Mayumi / Sekiya, Mizuki / Futai, Masamitsu

Biochimica et biophysica acta

2016 Volume 1857, Issue 2, Page(s) 129–140

Abstract	ATP synthases (FoF1) are found ubiquitously in energy-transducing membranes of bacteria, mitochondria, and chloroplasts. These enzymes couple proton transport and ATP synthesis or hydrolysis through subunit rotation, which has been studied mainly by observing single molecules. In this review, we discuss the mechanism of rotational catalysis of ATP synthases, mainly that from Escherichia coli, emphasizing the high-speed and stochastic rotation including variable rates and an inhibited state. Single molecule studies combined with structural information of the bovine mitochondrial enzyme and mutational analysis have been informative as to an understanding of the catalytic site and the interaction between rotor and stator subunits. We discuss the similarity and difference in structure and inhibitory regulation of F1 from bovine and E. coli. Unlike the crystal structure of bovine F1 (α3β3γ), that of E. coli contains a ε subunit, which is a known inhibitor of bacterial and chloroplast F1 ATPases. The carboxyl terminal domain of E. coli ε (εCTD) interacts with the catalytic and rotor subunits (β and γ, respectively), and then inhibits rotation. The effects of phytopolyphenols on F1-ATPase are also discussed: one of them, piceatannol, lowered the rotational speed by affecting rotor/stator interactions.
MeSH term(s)	Animals ; Biocatalysis ; Catalytic Domain ; Cattle ; Escherichia coli/chemistry ; Escherichia coli/drug effects ; Escherichia coli/enzymology ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Hydrolysis ; Models, Molecular ; Polyphenols/chemistry ; Polyphenols/pharmacology ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Protein Subunits/pharmacology ; Proton-Translocating ATPases/antagonists & inhibitors ; Proton-Translocating ATPases/chemistry ; Proton-Translocating ATPases/metabolism ; Rotation ; Species Specificity ; Thermodynamics
Chemical Substances	Escherichia coli Proteins ; Polyphenols ; Protein Subunits ; Proton-Translocating ATPases (EC 3.6.3.14)
Language	English
Publishing date	2016-02
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2015.11.005
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Article ; Online: Vacuolar-type ATPase: A proton pump to lysosomal trafficking.

Futai, Masamitsu / Sun-Wada, Ge-Hong / Wada, Yoh / Matsumoto, Naomi / Nakanishi-Matsui, Mayumi

Proceedings of the Japan Academy. Series B, Physical and biological sciences

2019 Volume 95, Issue 6, Page(s) 261–277

Abstract: Vacuolar-type ATPase (V-ATPase), initially identified in yeast and plant vacuoles, pumps protons into the lumen of organelles coupled with ATP hydrolysis. The mammalian counterpart is found ubiquitously in endomembrane organelles and the plasma membrane ... ...

Abstract	Vacuolar-type ATPase (V-ATPase), initially identified in yeast and plant vacuoles, pumps protons into the lumen of organelles coupled with ATP hydrolysis. The mammalian counterpart is found ubiquitously in endomembrane organelles and the plasma membrane of specialized cells such as osteoclasts. V-ATPase is also present in unique organelles such as insulin secretory granules, neural synaptic vesicles, and acrosomes of spermatozoa. Consistent with its diverse physiological roles and unique localization, the seven subunits of V-ATPase have 2-4 isoforms that are organelle- or cell-specific. Subunits of the enzyme function in trafficking organelles and vesicles by interacting with small molecule GTPases. During osteoclast differentiation, one of the four isoforms of subunit a, a3, is indispensable for secretory lysosome trafficking to the plasma membrane. Diseases such as osteopetrosis, renal acidosis, and hearing loss are related to V-ATPase isoforms. In addition to its role as an enzyme, V-ATPase has versatile physiological roles in eukaryotic cells.
MeSH term(s)	Animals ; Biological Transport ; Cell Membrane/metabolism ; Humans ; Lysosomes/metabolism ; Osteoclasts/cytology ; Vacuolar Proton-Translocating ATPases/metabolism
Chemical Substances	Vacuolar Proton-Translocating ATPases (EC 3.6.1.-)
Language	English
Publishing date	2019-06-11
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	161781-3
ISSN	1349-2896 ; 0386-2208
ISSN (online)	1349-2896
ISSN	0386-2208
DOI	10.2183/pjab.95.018
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Article ; Online: Role of α/β interface in F

Sekiya, Mizuki / Sakamoto, Yasumitsu / Futai, Masamitsu / Nakanishi-Matsui, Mayumi

International journal of biological macromolecules

2017 Volume 99, Page(s) 615–621

Abstract: ... The ... ...

Abstract	The F
MeSH term(s)	Animals ; Aurovertins/metabolism ; Aurovertins/pharmacology ; Binding Sites ; Biocatalysis ; Cattle ; Curcumin/metabolism ; Curcumin/pharmacology ; Drug Synergism ; Enzyme Inhibitors/metabolism ; Enzyme Inhibitors/pharmacology ; Escherichia coli/enzymology ; Hydrolysis ; Molecular Docking Simulation ; Mutation/drug effects ; Protein Conformation ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Proton-Translocating ATPases/antagonists & inhibitors ; Proton-Translocating ATPases/chemistry ; Proton-Translocating ATPases/genetics ; Proton-Translocating ATPases/metabolism ; Rotation
Chemical Substances	Aurovertins ; Enzyme Inhibitors ; Protein Subunits ; Proton-Translocating ATPases (EC 3.6.3.14) ; Curcumin (IT942ZTH98) ; citreoviridin (OWX7Q6CF4F)
Language	English
Publishing date	2017-06
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2017.02.089
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