LIVIVO - Search results -

Search results

Result 1 - 10 of total 38

Search options

Article ; Online: Protocol for imaging proteins associated with

Kitao, Tomoe / Arasaki, Kohei / Nagai, Hiroki / Kubori, Tomoko

STAR protocols

2021 Volume 2, Issue 2, Page(s) 100410

Abstract: The intracellular bacterial ... ...

Abstract	The intracellular bacterial pathogen
MeSH term(s)	Bacterial Proteins/analysis ; Bacterial Proteins/chemistry ; Bacteriological Techniques/methods ; Cell Culture Techniques ; Fluorescent Antibody Technique/methods ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Host-Pathogen Interactions/physiology ; Humans ; Legionella pneumophila/chemistry ; Plasmids/genetics ; Plasmids/metabolism ; Transfection ; Vacuoles/chemistry ; Vacuoles/microbiology
Chemical Substances	Bacterial Proteins ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2021-03-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2666-1667
ISSN (online)	2666-1667
DOI	10.1016/j.xpro.2021.100410
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Requirement of phosphatidic acid binding for distribution of the bacterial protein Lpg1137 targeting syntaxin 17.

Murata, Misaki / Kanamori, Riku / Kitao, Tomoe / Kubori, Tomoko / Nagai, Hiroki / Tagaya, Mitsuo / Arasaki, Kohei

Journal of cell science

2022 Volume 135, Issue 6

Abstract: The gram-negative bacterium, Legionella pneumophila is known to manipulate the host cellular functions. L. pneumophila secretes bacterial proteins called Legionella effectors into the host cytosol that are necessary for these manipulations. The ... ...

Abstract	The gram-negative bacterium, Legionella pneumophila is known to manipulate the host cellular functions. L. pneumophila secretes bacterial proteins called Legionella effectors into the host cytosol that are necessary for these manipulations. The Legionella effector Lpg1137 was identified as a serine protease responsible for the degradation of syntaxin 17 (Stx17). However, how Lpg1137 specifically recognizes and degrades Stx17 remained unknown. Given that Stx17 is localized in the ER, mitochondria-associated membrane (MAM), and mitochondria, Lpg1137 likely distributes to these compartments to recognize Stx17. Here, we show that the C-terminal region of Lpg1137 binds to phosphatidic acid (PA), a MAM and mitochondria-enriched phospholipid, and that this binding is required for the correct intracellular distribution of Lpg1137. Two basic residues in the C-terminal region of Lpg1137 are required for PA binding and their mutation causes mislocalization of Lpg1137. This mutant also fails to degrade Stx17 while retaining protease activity. Taken together, our data reveal that Lpg1137 utilizes PA for its distribution to the membranous compartments in which Stx17 is localized.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Legionella/metabolism ; Legionella pneumophila/genetics ; Legionella pneumophila/metabolism ; Phosphatidic Acids/metabolism ; Qa-SNARE Proteins/genetics ; Qa-SNARE Proteins/metabolism
Chemical Substances	Bacterial Proteins ; Phosphatidic Acids ; Qa-SNARE Proteins
Language	English
Publishing date	2022-03-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.259538
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 14: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Regulation of Mitochondrial Dynamics and Autophagy by the Mitochondria-Associated Membrane.

Tagaya, Mitsuo / Arasaki, Kohei

Advances in experimental medicine and biology

2017 Volume 997, Page(s) 33–47

Abstract: Mitochondria are powerhouses and central to metabolism in cells. They are highly dynamic organelles that continuously fuse, divide, and move along the cytoskeleton to form the mitochondrial network. The fusion and fission are catalyzed by four dynamin- ... ...

Abstract	Mitochondria are powerhouses and central to metabolism in cells. They are highly dynamic organelles that continuously fuse, divide, and move along the cytoskeleton to form the mitochondrial network. The fusion and fission are catalyzed by four dynamin-related GTPases in mammals that are controlled by a variety of protein-protein interactions and posttranslational modifications. Mitochondrial dynamics and metabolism are linked and regulate each other. Starvation induces mitochondrial elongation, which enables the mitochondria to produce energy more efficiently and to escape from autophagic degradation. Damaged portions of mitochondria are removed from the healthy parts by division, and subsequently degraded via a specific mode of autophagy termed mitophagy. Recent studies shed light on the contribution of the endoplasmic reticulum to mitochondrial dynamics and the cooperation of the two organelles for the progression of autophagy including mitophagy. A subdomain of the endoplasmic reticulum apposed to mitochondria is called the mitochondria-associated membrane (MAM), which comprises a unique set of proteins that interact with mitochondrial proteins. Here we review our current understanding of the molecular mechanisms of mitochondrial dynamics and mitochondria-related processes in the context of the interaction with the endoplasmic reticulum.
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-981-10-4567-7_3
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Legionella blocks autophagy by cleaving STX17 (syntaxin 17).

Arasaki, Kohei / Tagaya, Mitsuo

Autophagy

2017 Volume 13, Issue 11, Page(s) 2008–2009

Abstract: Pathogens subvert host defense systems including autophagy and apoptosis for their survival and proliferation. Legionella pneumophila is a Gram-negative bacterium that grows in alveolar macrophages and causes severe pneumonia. Early during infection ... ...

Abstract	Pathogens subvert host defense systems including autophagy and apoptosis for their survival and proliferation. Legionella pneumophila is a Gram-negative bacterium that grows in alveolar macrophages and causes severe pneumonia. Early during infection Legionella secretes effector proteins that convert the plasma membrane-derived vacuole containing Legionella into an endoplasmic reticulum (ER)-like replicative vacuole. These vacuoles ultimately fuse with the ER, where the pathogen replicates. Recently, we showed that one of the effectors, Lpg1137, is a serine protease that targets the mitochondria-associated ER membrane (MAM) and degrades STX17 (syntaxin 17), a SNARE implicated in macroautophagy/autophagy as well as mitochondria dynamics and membrane trafficking in fed cells. Degradation of STX17 blocks autophagy and BAX-induced apoptosis.
MeSH term(s)	Autophagy ; Legionella ; Legionella pneumophila ; Qa-SNARE Proteins ; Vacuoles
Chemical Substances	Qa-SNARE Proteins
Language	English
Publishing date	2017-09-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2017.1371395
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 6741: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: A MAP1B-cortactin-Tks5 axis regulates TNBC invasion and tumorigenesis.

The Journal of cell biology

2024 Volume 223, Issue 3

Abstract: The microtubule-associated protein MAP1B has been implicated in axonal growth and brain development. We found that MAP1B is highly expressed in the most aggressive and deadliest breast cancer subtype, triple-negative breast cancer (TNBC), but not in ... ...

Abstract	The microtubule-associated protein MAP1B has been implicated in axonal growth and brain development. We found that MAP1B is highly expressed in the most aggressive and deadliest breast cancer subtype, triple-negative breast cancer (TNBC), but not in other subtypes. Expression of MAP1B was found to be highly correlated with poor prognosis. Depletion of MAP1B in TNBC cells impairs cell migration and invasion concomitant with a defect in tumorigenesis. We found that MAP1B interacts with key components for invadopodia formation, cortactin, and Tks5, the latter of which is a PtdIns(3,4)P2-binding and scaffold protein that localizes to invadopodia. We also found that Tks5 associates with microtubules and supports the association between MAP1B and α-tubulin. In accordance with their interaction, depletion of MAP1B leads to Tks5 destabilization, leading to its degradation via the autophagic pathway. Collectively, these findings suggest that MAP1B is a convergence point of the cytoskeleton to promote malignancy in TNBC and thereby a potential diagnostic and therapeutic target for TNBC.
MeSH term(s)	Humans ; Carcinogenesis/genetics ; Cell Transformation, Neoplastic ; Cortactin/genetics ; Microtubule-Associated Proteins/genetics ; Triple Negative Breast Neoplasms/genetics ; MDA-MB-231 Cells ; Adaptor Proteins, Vesicular Transport/genetics ; Microtubules/metabolism ; Cytoskeleton/metabolism ; Female ; Animals ; Mice ; Mice, Inbred BALB C ; Podosomes/metabolism ; Tubulin/metabolism
Chemical Substances	Cortactin ; MAP1B protein, human ; Microtubule-Associated Proteins ; SH3PXD2A protein, human ; Adaptor Proteins, Vesicular Transport ; Tubulin
Language	English
Publishing date	2024-02-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202303102
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ub I Zs.190: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Legionella Manipulates Non-canonical SNARE Pairing Using a Bacterial Deubiquitinase.

Kitao, Tomoe / Taguchi, Kyoichiro / Seto, Shintaro / Arasaki, Kohei / Ando, Hiroki / Nagai, Hiroki / Kubori, Tomoko

Cell reports

2020 Volume 32, Issue 10, Page(s) 108107

Abstract: The intracellular bacterial pathogen Legionella pneumophila uses many effector proteins delivered by the bacterial type IV secretion system (T4SS) to hijack the early secretory pathway to establish its replicative niche, known as the Legionella- ... ...

Abstract	The intracellular bacterial pathogen Legionella pneumophila uses many effector proteins delivered by the bacterial type IV secretion system (T4SS) to hijack the early secretory pathway to establish its replicative niche, known as the Legionella-containing vacuole (LCV). On LCV biogenesis, the endoplasmic reticulum (ER) vesicular soluble N-ethylmaleimide-sensitive factor attachment protein receptors (v-SNARE) Sec22b is recruited to the bacterial phagosome and forms non-canonical pairings with target membrane SNAREs (t-SNAREs) from the plasma membrane. Here, we identify a Legionella deubiquitinase (DUB), LotB, that can modulate the early secretory pathway by interacting with coatomer protein complex I (COPI) vesicles when ectopically expressed. We show that Sec22b is ubiquitinated upon L. pneumophila infection in a T4SS-dependent manner and that, subsequently, LotB deconjugates K63-linked ubiquitins from Sec22b. The DUB activity of LotB stimulates dissociation of the t-SNARE syntaxin 3 (Stx3) from Sec22b, which resides on the LCV. Our study highlights a bacterial strategy manipulating the dynamics of infection-induced SNARE pairing using a bacterial DUB.
MeSH term(s)	Bacterial Proteins/metabolism ; Deubiquitinating Enzymes/metabolism ; Legionella pneumophila/pathogenicity ; Transfection
Chemical Substances	Bacterial Proteins ; Deubiquitinating Enzymes (EC 3.4.19.12)
Language	English
Publishing date	2020-08-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.108107
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Legionella

Arasaki, Kohei / Kimura, Hana / Tagaya, Mitsuo / Roy, Craig R

The Journal of cell biology

2018 Volume 217, Issue 11, Page(s) 3863–3872

Abstract: During the initial stage of infection, ...

Abstract	During the initial stage of infection,
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Cell Membrane/microbiology ; Cell Membrane/pathology ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/microbiology ; Endoplasmic Reticulum/pathology ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; HEK293 Cells ; Humans ; Legionella pneumophila/genetics ; Legionella pneumophila/metabolism ; Legionnaires' Disease/genetics ; Legionnaires' Disease/metabolism ; Legionnaires' Disease/pathology ; Vacuoles/genetics ; Vacuoles/metabolism ; Vacuoles/microbiology ; Vacuoles/pathology ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism ; rab1 GTP-Binding Proteins/genetics ; rab1 GTP-Binding Proteins/metabolism
Chemical Substances	Bacterial Proteins ; EXOC2 protein, human ; EXOC6B protein, human ; Guanine Nucleotide Exchange Factors ; SidM protein, Legionella pneumophila ; Vesicular Transport Proteins ; GTP-Binding Proteins (EC 3.6.1.-) ; rab1 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2018-10-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201801208
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ub I Zs.190: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Legionella hijacks the host Golgi-to-ER retrograde pathway for the association of Legionella-containing vacuole with the ER.

Kawabata, Mio / Matsuo, Honoka / Koito, Takumi / Murata, Misaki / Kubori, Tomoko / Nagai, Hiroki / Tagaya, Mitsuo / Arasaki, Kohei

PLoS pathogens

2021 Volume 17, Issue 3, Page(s) e1009437

Abstract: Legionella pneumophila (L. pneumophila) is a gram-negative bacterium that replicates in a compartment that resembles the host endoplasmic reticulum (ER). To create its replicative niche, L. pneumophila manipulates host membrane traffic and fusion ... ...

Abstract	Legionella pneumophila (L. pneumophila) is a gram-negative bacterium that replicates in a compartment that resembles the host endoplasmic reticulum (ER). To create its replicative niche, L. pneumophila manipulates host membrane traffic and fusion machineries. Bacterial proteins called Legionella effectors are translocated into the host cytosol and play a crucial role in these processes. In an early stage of infection, Legionella subverts ER-derived vesicles (ERDVs) by manipulating GTPase Rab1 to facilitate remodeling of the Legionella-containing vacuole (LCV). Subsequently, the LCV associates with the ER in a mechanism that remains elusive. In this study, we show that L. pneumophila recruits GTPases Rab33B and Rab6A, which regulate vesicle trafficking from the Golgi to the ER, to the LCV to promote the association of LCV with the ER. We found that recruitment of Rab6A to the LCV depends on Rab33B. Legionella effector SidE family proteins, which phosphoribosyl-ubiquitinate Rab33B, were found to be necessary for the recruitment of Rab33B to the LCV. Immunoprecipitation experiments revealed that L. pneumophila facilitates the interaction of Rab6 with ER-resident SNAREs comprising syntaxin 18, p31, and BNIP1, but not tethering factors including NAG, RINT-1, and ZW10, which are normally required for syntaxin 18-mediated fusion of Golgi-derived vesicles with the ER. Our results identified a Rab33B-Rab6A cascade on the LCV and the interaction of Rab6 with ER-resident SNARE proteins for the association of LCV with the ER and disclosed the unidentified physiological role of SidE family proteins.
MeSH term(s)	Bacterial Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/microbiology ; Golgi Apparatus/metabolism ; Golgi Apparatus/microbiology ; HEK293 Cells ; HeLa Cells ; Humans ; Legionella pneumophila/metabolism ; Legionella pneumophila/pathogenicity ; Legionnaires' Disease/metabolism ; Protein Transport/physiology ; Vacuoles/metabolism ; Vacuoles/microbiology
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2021-03-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1009437
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3.

Kimura, Hana / Arasaki, Kohei / Ohsaki, Yuki / Fujimoto, Toyoshi / Ohtomo, Takayuki / Yamada, Junji / Tagaya, Mitsuo

Journal of lipid research

2018 Volume 59, Issue 5, Page(s) 805–819

Abstract: Lipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigations. ... ...

Abstract	Lipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigations. In the present study, we show that syntaxin 17 (Stx17), a soluble
MeSH term(s)	3T3-L1 Cells ; Animals ; Cells, Cultured ; Coenzyme A Ligases/metabolism ; Female ; HEK293 Cells ; Hep G2 Cells ; Humans ; Lipid Droplets/metabolism ; Mice ; Qa-SNARE Proteins/metabolism
Chemical Substances	Qa-SNARE Proteins ; Coenzyme A Ligases (EC 6.2.1.-) ; long-chain-fatty-acid-CoA ligase (EC 6.2.1.3)
Language	English
Publishing date	2018-03-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1194/jlr.M081679
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 175: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Moonlighting functions of the NRZ (mammalian Dsl1) complex.

Tagaya, Mitsuo / Arasaki, Kohei / Inoue, Hiroki / Kimura, Hana

Frontiers in cell and developmental biology

2014 Volume 2, Page(s) 25

Abstract: The yeast Dsl1 complex, which comprises Dsl1, Tip20, and Sec39/Dsl3, has been shown to participate, as a vesicle-tethering complex, in retrograde trafficking from the Golgi apparatus to the endoplasmic reticulum. Its metazoan counterpart NRZ complex, ... ...

Abstract	The yeast Dsl1 complex, which comprises Dsl1, Tip20, and Sec39/Dsl3, has been shown to participate, as a vesicle-tethering complex, in retrograde trafficking from the Golgi apparatus to the endoplasmic reticulum. Its metazoan counterpart NRZ complex, which comprises NAG, RINT1, and ZW10, is also involved in Golgi-to-ER retrograde transport, but each component of the complex has diverse cellular functions including endosome-to-Golgi transport, cytokinesis, cell cycle checkpoint, autophagy, and mRNA decay. In this review, we summarize the current knowledge of the metazoan NRZ complex and discuss the "moonlighting" functions and intercorrelation of their subunits.
Language	English
Publishing date	2014-06-11
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2014.00025
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

To top

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito