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Article ; Online: Unique E2-binding specificity of artificial RING fingers in cancer cells.

Miyamoto, Kazuhide / Tadokoro, Takashi / Matsumoto, Atsushi

2024 Volume 14, Issue 1, Page(s) 2545

Abstract: Ubiquitin (Ub)-conjugating enzymes (E2s) are involved in various pathways for Ub transfer and deubiquitinating activities. These enzymes are associated with cancers such as breast cancer which is the second deadliest type of malignancy among women. Here, ...

Abstract	Ubiquitin (Ub)-conjugating enzymes (E2s) are involved in various pathways for Ub transfer and deubiquitinating activities. These enzymes are associated with cancers such as breast cancer which is the second deadliest type of malignancy among women. Here, we revealed the unique E2-binding property and the auto-ubiquitination of artificial RING fingers (ARFs). Circular dichroism spectra showed the characteristic structures of ARFs. The proline, lysine, leucine, threonine and cysteine (PKLTC) sequence of ARF was important for E2-recognition and its mutations induced obvious changes in the E2-binding specificity and the auto-ubiquitination activity of ARF. The ARF mutants were applicable to detection of most of E2 activities. Furthermore, adding the ARF mutant C35A to cancer cells promoted its auto-ubiquitination, leading to the preferential detection of E2 UbcH5b activity. The present work opens up a new avenue for investigating intracellular E2 activities for the fatal diseases.
MeSH term(s)	Female ; Humans ; Ubiquitination ; Ubiquitin-Conjugating Enzymes/metabolism ; Breast Neoplasms/genetics ; Ubiquitin-Protein Ligases/metabolism ; Protein Binding
Chemical Substances	Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2024-01-31
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-52793-y
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Article ; Online: Protein kinase Cβ is involved in cigarette smoke gas phase-induced ferroptosis in J774 macrophages.

Higashi, Tsunehito / Handa, Haruka / Mai, Yosuke / Maenaka, Katsumi / Tadokoro, Takashi

Journal of pharmacological sciences

2023 Volume 153, Issue 1, Page(s) 22–25

Abstract: Cigarette smoking is a risk factor for respiratory infection caused by immune cell dysfunction. Cigarette smoke is divided into tar and gas phases. Although the gas phase induces cell death in various cell types, the mechanism for gas phase-induced cell ... ...

Abstract	Cigarette smoking is a risk factor for respiratory infection caused by immune cell dysfunction. Cigarette smoke is divided into tar and gas phases. Although the gas phase induces cell death in various cell types, the mechanism for gas phase-induced cell death remains to be clarified. In this study, we have examined the effects of cigarette smoke gas phase on J774 macrophages. Cigarette smoke gas phase and cytotoxic factors in the gas phase induced protein kinase C (PKC)-dependent ferroptosis. Pharmacological studies using isoform-specific PKC inhibitors have revealed that PKCβ is involved in cigarette smoke gas phase-induced ferroptosis in J774 macrophages.
Language	English
Publishing date	2023-06-21
Publishing country	Japan
Document type	Journal Article
ZDB-ID	2104264-0
ISSN	1347-8648 ; 1347-8613
ISSN (online)	1347-8648
ISSN	1347-8613
DOI	10.1016/j.jphs.2023.06.001
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Article ; Online: Low-Cost Cell-Surface-Mimic Analysis of Ligand Interactions of Biotinylated Immune Receptors Using Surface Plasmon Resonance.

Kuroki, Kimiko / Fukuhara, Hideo / Tadokoro, Takashi / Maenaka, Katsumi

Methods in molecular biology (Clifton, N.J.)

2021 Volume 2421, Page(s) 21–35

Abstract: On the immune cell surface, many immune receptors are expressed and modulate the inhibitory or activating signals to control the immune responses. Recently, some of these receptors have been categorized as immune checkpoint receptors and targeted for ... ...

Abstract	On the immune cell surface, many immune receptors are expressed and modulate the inhibitory or activating signals to control the immune responses. Recently, some of these receptors have been categorized as immune checkpoint receptors and targeted for cancer immunity or autoimmune diseases. To analyze the weak and fast binding typical for immune receptor-ligand interactions, a real-time surface plasmon resonance (SPR) technique is useful. However, it sometimes becomes difficult to optimize the immobilization conditions and appropriate controls. Considering that receptor orientation is relevant for achieving function on the cell surface, it is important to immobilize ligand proteins using specific tags at the membrane proximal end to avoid steric hindrance and structural changes in specific binding regions. Here we introduce a sensor chip, Sensor Chip CAP (Cytiva), which enables reversible and orientation-controlled immobilization of biotinylated ligands, resulting in a significant cost-effective method. We further show preparation methods of several biotinylated immune receptor proteins for SPR analysis, which are also useful for structural and other functional analyses.
MeSH term(s)	Ligands ; Oligonucleotide Array Sequence Analysis ; Receptors, Immunologic ; Surface Plasmon Resonance
Chemical Substances	Ligands ; Receptors, Immunologic
Language	English
Publishing date	2021-12-06
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1944-5_2
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Article ; Online: Cysteine-Rich Secretory Proteins (CRISPs) From Venomous Snakes: An Overview of the Functional Diversity in A Large and Underappreciated Superfamily.

Tadokoro, Takashi / Modahl, Cassandra M / Maenaka, Katsumi / Aoki-Shioi, Narumi

Toxins

2020 Volume 12, Issue 3

Abstract: The CAP protein superfamily (Cysteine-rich secretory proteins (CRISPs), Antigen 5 (Ag5), and Pathogenesis-related 1 (PR-1) proteins) is widely distributed, but for toxinologists, snake venom CRISPs are the most familiar members. Although CRISPs are found ...

Abstract	The CAP protein superfamily (Cysteine-rich secretory proteins (CRISPs), Antigen 5 (Ag5), and Pathogenesis-related 1 (PR-1) proteins) is widely distributed, but for toxinologists, snake venom CRISPs are the most familiar members. Although CRISPs are found in the majority of venoms, very few of these proteins have been functionally characterized, but those that have been exhibit diverse activities. Snake venom CRISPs (svCRISPs) inhibit ion channels and the growth of new blood vessels (angiogenesis). They also increase vascular permeability and promote inflammatory responses (leukocyte and neutrophil infiltration). Interestingly, CRISPs in lamprey buccal gland secretions also manifest some of these activities, suggesting an evolutionarily conserved function. As we strive to better understand the functions that CRISPs serve in venoms, it is worth considering the broad range of CRISP physiological activities throughout the animal kingdom. In this review, we summarize those activities, known crystal structures and sequence alignments, and we discuss predicted functional sites. CRISPs may not be lethal or major components of venoms, but given their almost ubiquitous occurrence in venoms and the accelerated evolution of svCRISP genes, these venom proteins are likely to have functions worth investigating.
MeSH term(s)	Animals ; Cysteine ; Evolution, Molecular ; Humans ; Protein Binding ; Reptilian Proteins/chemistry ; Reptilian Proteins/genetics ; Reptilian Proteins/toxicity ; Snake Venoms/chemistry ; Snake Venoms/genetics ; Snake Venoms/toxicity
Chemical Substances	Reptilian Proteins ; Snake Venoms ; Cysteine (K848JZ4886)
Language	English
Publishing date	2020-03-12
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2518395-3
ISSN	2072-6651 ; 2072-6651
ISSN (online)	2072-6651
ISSN	2072-6651
DOI	10.3390/toxins12030175
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Article ; Online: Correction: Synthesis of glycerolipids containing simple linear acyl chains or aromatic rings and evaluation of their Mincle signaling activity.

Matsumaru, Takanori / Ikeno, Risa / Shuchi, Yusuke / Iwamatsu, Toshiki / Tadokoro, Takashi / Yamasaki, Sho / Fujimoto, Yukari / Furukawa, Atsushi / Maenaka, Katsumi

Chemical communications (Cambridge, England)

2022 Volume 58, Issue 15, Page(s) 2580

Abstract: Correction for 'Synthesis of glycerolipids containing simple linear acyl chains or aromatic rings and evaluation of their Mincle signaling activity' by Takanori ... ...

Abstract	Correction for 'Synthesis of glycerolipids containing simple linear acyl chains or aromatic rings and evaluation of their Mincle signaling activity' by Takanori Matsumaru
Language	English
Publishing date	2022-02-17
Publishing country	England
Document type	Published Erratum
ZDB-ID	1472881-3
ISSN	1364-548X ; 1359-7345 ; 0009-241X
ISSN (online)	1364-548X
ISSN	1359-7345 ; 0009-241X
DOI	10.1039/d2cc90023h
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Article ; Online: Identification of RPL15 60S Ribosomal Protein as a Novel Topotecan Target Protein That Correlates with DAMP Secretion and Antitumor Immune Activation.

Yamada, Shunsuke / Kitai, Yuichi / Tadokoro, Takashi / Takahashi, Runa / Shoji, Haruka / Maemoto, Taiga / Ishiura, Marie / Muromoto, Ryuta / Kashiwakura, Jun-Ichi / Ishii, Ken J / Maenaka, Katsumi / Kawai, Taro / Matsuda, Tadashi

Journal of immunology (Baltimore, Md. : 1950)

2022 Volume 209, Issue 1, Page(s) 171–179

Abstract: Damage-associated molecular patterns (DAMPs) contribute to antitumor immunity during cancer chemotherapy. We previously demonstrated that topotecan (TPT), a topoisomerase I inhibitor, induces DAMP secretion from cancer cells, which activates STING- ... ...

Abstract	Damage-associated molecular patterns (DAMPs) contribute to antitumor immunity during cancer chemotherapy. We previously demonstrated that topotecan (TPT), a topoisomerase I inhibitor, induces DAMP secretion from cancer cells, which activates STING-mediated antitumor immune responses. However, how TPT induces DAMP secretion in cancer cells is yet to be elucidated. Here, we identified RPL15, a 60S ribosomal protein, as a novel TPT target and showed that TPT inhibited preribosomal subunit formation via its binding to RPL15, resulting in the induction of DAMP-mediated antitumor immune activation independent of TOP1. TPT inhibits RPL15-RPL4 interactions and decreases RPL4 stability, which is recovered by CDK12 activity.
MeSH term(s)	Animals ; Mice ; Neoplasms/drug therapy ; Ribosomal Proteins ; Topoisomerase I Inhibitors/pharmacology ; Topotecan/pharmacology ; Topotecan/therapeutic use
Chemical Substances	Ribosomal Proteins ; Topoisomerase I Inhibitors ; Topotecan (7M7YKX2N15)
Language	English
Publishing date	2022-06-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.2100963
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Ud II Zs.37: 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)
Zs.MG 28: Show issues

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Article ; Online: Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation.

Hirao, Kengo / Andrews, Sophie / Kuroki, Kimiko / Kusaka, Hiroki / Tadokoro, Takashi / Kita, Shunsuke / Ose, Toyoyuki / Rowland-Jones, Sarah L / Maenaka, Katsumi

iScience

2019 Volume 23, Issue 1, Page(s) 100758

Abstract: The human immunodeficiency virus (HIV) accessory protein Nef plays a major role in establishing and maintaining infection, particularly through immune evasion. Many HIV-2-infected people experience long-term viral control and survival, resembling HIV-1 ... ...

Abstract	The human immunodeficiency virus (HIV) accessory protein Nef plays a major role in establishing and maintaining infection, particularly through immune evasion. Many HIV-2-infected people experience long-term viral control and survival, resembling HIV-1 elite control. HIV-2 Nef has overlapping but also distinct functions from HIV-1 Nef. Here we report the crystal structure of HIV-2 Nef core. The di-leucine sorting motif forms a helix bound to neighboring molecules, and moreover, isothermal titration calorimetry demonstrated that the CD3 endocytosis motif can directly bind to HIV-2 Nef, ensuring AP-2-mediated endocytosis for CD3. The highly conserved C-terminal region forms a α-helix, absent from HIV-1. We further determined the structure of simian immunodeficiency virus (SIV) Nef harboring this region, demonstrating similar C-terminal α-helix, which may contribute to AP-1 binding for MHC-I downregulation. These results provide insights into the distinct pathogenesis of HIV-2 infection.
Language	English
Publishing date	2019-12-09
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2019.100758
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Article ; Online: RECQL5 plays co-operative and complementary roles with WRN syndrome helicase.

Popuri, Venkateswarlu / Huang, Jing / Ramamoorthy, Mahesh / Tadokoro, Takashi / Croteau, Deborah L / Bohr, Vilhelm A

Nucleic acids research

2017 Volume 45, Issue 3, Page(s) 1566

Abstract: Humans have five RecQ helicases, whereas simpler organisms have only one. Little is known about whether and how these RecQ helicases co-operate and/or complement each other in response to cellular stress. Here we show that RECQL5 associates longer at ... ...

Abstract	Humans have five RecQ helicases, whereas simpler organisms have only one. Little is known about whether and how these RecQ helicases co-operate and/or complement each other in response to cellular stress. Here we show that RECQL5 associates longer at laser-induced DNA double-strand breaks in the absence of Werner syndrome (WRN) protein, and that it interacts physically and functionally with WRN both in vivo and in vitro. RECQL5 co-operates with WRN on synthetic stalled replication fork-like structures and stimulates its helicase activity on DNA fork duplexes. Both RECQL5 and WRN re-localize from the nucleolus into the nucleus after replicative stress and significantly associate with each other during S-phase. Further, we show that RECQL5 is essential for cell survival in the absence of WRN. Loss of both RECQL5 and WRN severely compromises DNA replication, accumulates genomic instability and ultimately leads to cell death. Collectively, our results indicate that RECQL5 plays both co-operative and complementary roles with WRN. This is an early demonstration of a significant functional interplay and a novel synthetic lethal interaction among the human RecQ helicases.
Language	English
Publishing date	2017-02-09
Publishing country	England
Document type	Journal Article ; Published Erratum
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkw1216
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Article ; Online: Relation of Colloidal and Conformational Stabilities to Aggregate Formation in a Monoclonal Antibody.

Oyama, Hiroaki / Koga, Hiroki / Tadokoro, Takashi / Maenaka, Katsumi / Shiota, Akira / Yokoyama, Masami / Noda, Masanori / Torisu, Tetsuo / Uchiyama, Susumu

Journal of pharmaceutical sciences

2019 Volume 109, Issue 1, Page(s) 308–315

Abstract: Aggregation of therapeutic monoclonal antibodies has a potential risk of immunogenicity, requiring minimization of aggregate formation. We have developed a fitting formula for antibody aggregation at 40°C based on physicochemical parameters, including ... ...

Abstract	Aggregation of therapeutic monoclonal antibodies has a potential risk of immunogenicity, requiring minimization of aggregate formation. We have developed a fitting formula for antibody aggregation at 40°C based on physicochemical parameters, including colloidal and conformational stabilities. An IgG1 monoclonal antibody, MAb-T, was formulated in 24 combinations of different buffer types and pH with or without sodium chloride. The fitting formula for monomer loss was successfully established by nonlinear regression analysis of the results from accelerated stability testing. Calculated monomer fraction values by the fitting formula were strongly correlated with experimental values (R
MeSH term(s)	Antibodies, Monoclonal/chemistry ; Buffers ; Calorimetry, Differential Scanning ; Chromatography, Gel ; Drug Compounding ; Hydrogen-Ion Concentration ; Immunoglobulin G/chemistry ; Mass Spectrometry ; Models, Chemical ; Protein Aggregates ; Protein Conformation ; Protein Stability ; Protein Unfolding ; Sodium Acetate/chemistry ; Temperature
Chemical Substances	Antibodies, Monoclonal ; Buffers ; Immunoglobulin G ; Protein Aggregates ; Sodium Acetate (4550K0SC9B)
Language	English
Publishing date	2019-10-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3151-3
ISSN	1520-6017 ; 0022-3549
ISSN (online)	1520-6017
ISSN	0022-3549
DOI	10.1016/j.xphs.2019.10.038
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Article ; Online: Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes.

Tadokoro, Takashi / Kanaya, Shigenori

The FEBS journal

2009 Volume 276, Issue 6, Page(s) 1482–1493

Abstract: The prokaryotic genomes, for which complete nucleotide sequences are available, always contain at least one RNase H gene, indicating that RNase H is ubiquitous in all prokaryotic cells. Coupled with its unique substrate specificity, the enzyme has been ... ...

Abstract	The prokaryotic genomes, for which complete nucleotide sequences are available, always contain at least one RNase H gene, indicating that RNase H is ubiquitous in all prokaryotic cells. Coupled with its unique substrate specificity, the enzyme has been expected to play crucial roles in the biochemical processes associated with DNA replication, gene expression and DNA repair. The physiological role of prokaryotic RNases H, especially of type 1 RNases H, has been extensively studied using Escherichia coli strains that are defective in RNase HI activity or overproduce RNase HI. However, it is not fully understood yet. By contrast, significant progress has been made in this decade in identifying novel RNases H with respect to their biochemical properties and structures, and elucidating catalytic mechanism and substrate recognition mechanism of RNase H. We review the results of these studies.
MeSH term(s)	Archaea/enzymology ; Archaea/genetics ; Bacteria/enzymology ; Bacteria/genetics ; Biocatalysis ; Genome, Archaeal ; Genome, Bacterial ; Models, Molecular ; Ribonuclease H/chemistry ; Ribonuclease H/metabolism ; Substrate Specificity
Chemical Substances	Ribonuclease H (EC 3.1.26.4)
Language	English
Publishing date	2009-03
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2009.06907.x
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