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Article ; Online: Soluble SLAMF7 is a predictive biomarker for elotuzumab therapy.

Suzuki, Atsushi / Kakugawa, Satoshi / Miyoshi, Masafumi / Hori, Mitsuo / Suzuki, Kenshi / Furukawa, Yusuke / Ohta, Kensuke

Leukemia

2020 Volume 34, Issue 11, Page(s) 3088–3090

MeSH term(s)	Antibodies, Monoclonal, Humanized/administration & dosage ; Antibodies, Monoclonal, Humanized/adverse effects ; Antibodies, Monoclonal, Humanized/drug effects ; Antineoplastic Agents, Immunological/administration & dosage ; Antineoplastic Agents, Immunological/adverse effects ; Antineoplastic Agents, Immunological/therapeutic use ; Biomarkers, Tumor ; Humans ; Multiple Myeloma/blood ; Multiple Myeloma/diagnosis ; Multiple Myeloma/drug therapy ; Prognosis ; Signaling Lymphocytic Activation Molecule Family/blood ; Treatment Outcome
Chemical Substances	Antibodies, Monoclonal, Humanized ; Antineoplastic Agents, Immunological ; Biomarkers, Tumor ; SLAMF7 protein, human ; Signaling Lymphocytic Activation Molecule Family ; elotuzumab (1351PE5UGS)
Language	English
Publishing date	2020-05-12
Publishing country	England
Document type	Letter ; Research Support, Non-U.S. Gov't
ZDB-ID	807030-1
ISSN	1476-5551 ; 0887-6924
ISSN (online)	1476-5551
ISSN	0887-6924
DOI	10.1038/s41375-020-0860-7
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Article ; Online: Making, Exporting, and Modulating Wnts.

Langton, Paul F / Kakugawa, Satoshi / Vincent, Jean-Paul

Trends in cell biology

2016 Volume 26, Issue 10, Page(s) 756–765

Abstract: Wnt proteins activate a conserved signalling pathway that controls development and tissue homeostasis in all metazoans. The intensity of Wnt signalling must be tightly controlled to avoid diseases caused by excess or ectopic signalling. Over the years, ... ...

Abstract	Wnt proteins activate a conserved signalling pathway that controls development and tissue homeostasis in all metazoans. The intensity of Wnt signalling must be tightly controlled to avoid diseases caused by excess or ectopic signalling. Over the years, many proteins dedicated to Wnt function have been identified, including Porcupine, which appends a palmitoleate moiety that is essential for signalling activity. This lipid inevitably affects subcellular trafficking and solubility, as well as providing a target for post-translational modulation. We review here the life history of Wnts, starting with progression through the secretory pathway, continuing with release and spread in the extracellular space, and finishing with the various proteins that dampen or inactivate Wnts in the extracellular space.
Language	English
Publishing date	2016-10
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2016.05.011
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Article ; Online: Notum deacylates octanoylated ghrelin.

Zhao, Yuguang / Schuhmacher, Laura-Nadine / Roberts, Morgan / Kakugawa, Satoshi / Bineva-Todd, Ganka / Howell, Steve / O'Reilly, Nicola / Perret, Christine / Snijders, Ambrosius P / Vincent, Jean-Paul / Jones, E Yvonne

Molecular metabolism

2021 Volume 49, Page(s) 101201

Abstract: Objectives: The only proteins known to be modified by O-linked lipidation are Wnts and ghrelin, and enzymatic removal of this post-translational modification inhibits ligand activity. Indeed, the Wnt-deacylase activity of Notum is the basis of its ... ...

Abstract	Objectives: The only proteins known to be modified by O-linked lipidation are Wnts and ghrelin, and enzymatic removal of this post-translational modification inhibits ligand activity. Indeed, the Wnt-deacylase activity of Notum is the basis of its ability to act as a feedback inhibitor of Wnt signalling. Whether Notum also deacylates ghrelin has not been determined. Methods: We used mass spectrometry to assay ghrelin deacylation by Notum and co-crystallisation to reveal enzyme-substrate interactions at the atomic level. CRISPR/Cas technology was used to tag endogenous Notum and assess its localisation in mice while liver-specific Notum knock-out mice allowed us to investigate the physiological role of Notum in modulating the level of ghrelin deacylation. Results: Mass spectrometry detected the removal of octanoyl from ghrelin by purified active Notum but not by an inactive mutant. The 2.2 Å resolution crystal structure of the Notum-ghrelin complex showed that the octanoyl lipid was accommodated in the hydrophobic pocket of the Notum. The knock-in allele expressing HA-tagged Notum revealed that Notum was produced in the liver and present in the bloodstream, albeit at a low level. Liver-specific inactivation of Notum in animals fed a high-fat diet led to a small but significant increase in acylated ghrelin in the circulation, while no such increase was seen in wild-type animals on the same diet. Conclusions: Overall, our data demonstrate that Notum can act as a ghrelin deacylase, and that this may be physiologically relevant under high-fat diet conditions. Our study therefore adds Notum to the list of enzymes, including butyrylcholinesterase and other carboxylesterases, that modulate the acylation state of ghrelin. The contribution of multiple enzymes could help tune the activity of this important hormone to a wide range of physiological conditions.
MeSH term(s)	Acylation ; Animals ; Butyrylcholinesterase/metabolism ; Esterases/chemistry ; Esterases/genetics ; Esterases/metabolism ; Ghrelin/genetics ; Ghrelin/metabolism ; Humans ; Ligands ; Male ; Mice ; Mice, Knockout
Chemical Substances	GHRL protein, human ; Ghrelin ; Ligands ; Esterases (EC 3.1.-) ; Notum protein, human (EC 3.1.1.-) ; Notum protein, mouse (EC 3.1.1.-) ; Butyrylcholinesterase (EC 3.1.1.8)
Language	English
Publishing date	2021-02-27
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2708735-9
ISSN	2212-8778 ; 2212-8778
ISSN (online)	2212-8778
ISSN	2212-8778
DOI	10.1016/j.molmet.2021.101201
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Article ; Online: Notum deacylates octanoylated ghrelin

Yuguang Zhao / Laura-Nadine Schuhmacher / Morgan Roberts / Satoshi Kakugawa / Ganka Bineva-Todd / Steve Howell / Nicola O'Reilly / Christine Perret / Ambrosius P. Snijders / Jean-Paul Vincent / E. Yvonne Jones

Molecular Metabolism, Vol 49, Iss , Pp 101201- (2021)

2021

Abstract	Objectives: The only proteins known to be modified by O-linked lipidation are Wnts and ghrelin, and enzymatic removal of this post-translational modification inhibits ligand activity. Indeed, the Wnt-deacylase activity of Notum is the basis of its ability to act as a feedback inhibitor of Wnt signalling. Whether Notum also deacylates ghrelin has not been determined. Methods: We used mass spectrometry to assay ghrelin deacylation by Notum and co-crystallisation to reveal enzyme–substrate interactions at the atomic level. CRISPR/Cas technology was used to tag endogenous Notum and assess its localisation in mice while liver-specific Notum knock-out mice allowed us to investigate the physiological role of Notum in modulating the level of ghrelin deacylation. Results: Mass spectrometry detected the removal of octanoyl from ghrelin by purified active Notum but not by an inactive mutant. The 2.2 Å resolution crystal structure of the Notum-ghrelin complex showed that the octanoyl lipid was accommodated in the hydrophobic pocket of the Notum. The knock-in allele expressing HA-tagged Notum revealed that Notum was produced in the liver and present in the bloodstream, albeit at a low level. Liver-specific inactivation of Notum in animals fed a high-fat diet led to a small but significant increase in acylated ghrelin in the circulation, while no such increase was seen in wild-type animals on the same diet. Conclusions: Overall, our data demonstrate that Notum can act as a ghrelin deacylase, and that this may be physiologically relevant under high-fat diet conditions. Our study therefore adds Notum to the list of enzymes, including butyrylcholinesterase and other carboxylesterases, that modulate the acylation state of ghrelin. The contribution of multiple enzymes could help tune the activity of this important hormone to a wide range of physiological conditions.
Keywords	Notum ; Ghrelin ; Deacylation ; Crystal structure ; Metabolism ; Internal medicine ; RC31-1245
Subject code	570
Language	English
Publishing date	2021-07-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Oseltamivir Is Effective against 1918 Influenza Virus Infection of Macaques but Vulnerable to Escape.

Feldmann, Friederike / Kobasa, Darwyn / Embury-Hyatt, Carissa / Grolla, Allen / Taylor, Tracy / Kiso, Maki / Kakugawa, Satoshi / Gren, Jason / Jones, Steven M / Kawaoka, Yoshihiro / Feldmann, Heinz

mBio

2019 Volume 10, Issue 5

Abstract: The 1918 influenza virus, subtype H1N1, was the causative agent of the most devastating pandemic in the history of infectious diseases. ...

Abstract	The 1918 influenza virus, subtype H1N1, was the causative agent of the most devastating pandemic in the history of infectious diseases.
MeSH term(s)	Animals ; Influenza A Virus, H1N1 Subtype/drug effects ; Influenza A Virus, H1N1 Subtype/pathogenicity ; Macaca ; Orthomyxoviridae Infections/drug therapy ; Orthomyxoviridae Infections/virology ; Oseltamivir/therapeutic use
Chemical Substances	Oseltamivir (20O93L6F9H)
Language	English
Publishing date	2019-10-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.02059-19
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Article ; Online: Competitive incorporation of homologous gene segments of influenza A virus into virions.

Inagaki, Arisa / Goto, Hideo / Kakugawa, Satoshi / Ozawa, Makoto / Kawaoka, Yoshihiro

Journal of virology

2012 Volume 86, Issue 18, Page(s) 10200–10202

Abstract: By using two reporter protein-encoding virus-like RNAs derived from identical viral RNA (vRNA) segments, we assessed their incorporation efficiency into single progeny virions. Most plaques formed by the recombinant viruses that were generated in cells ... ...

Abstract	By using two reporter protein-encoding virus-like RNAs derived from identical viral RNA (vRNA) segments, we assessed their incorporation efficiency into single progeny virions. Most plaques formed by the recombinant viruses that were generated in cells positive for both reporter genes expressed only one or the other protein. These results suggest that two virus-like RNAs encoding different reporter proteins compete for incorporation into virions, and individual influenza virions incorporate single, but not multiple, copies of homologous vRNA segments.
MeSH term(s)	Animals ; Cell Line ; Dogs ; Genes, Reporter ; Genes, Viral ; Humans ; Influenza A virus/genetics ; Influenza A virus/physiology ; Neuraminidase/genetics ; Plasmids/genetics ; RNA, Viral/genetics ; RNA-Dependent RNA Polymerase/genetics ; Recombinant Proteins/genetics ; Transfection ; Viral Proteins/genetics ; Virion/genetics ; Virion/physiology ; Virus Assembly/genetics ; Virus Assembly/physiology
Chemical Substances	PB2 protein, Influenzavirus A ; RNA, Viral ; Recombinant Proteins ; Viral Proteins ; RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; NA protein, influenza A virus (EC 3.2.1.18) ; Neuraminidase (EC 3.2.1.18)
Language	English
Publishing date	2012-06-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01204-12
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Article ; Online: Godzilla-dependent transcytosis promotes Wingless signalling in Drosophila wing imaginal discs.

Yamazaki, Yasuo / Palmer, Lucy / Alexandre, Cyrille / Kakugawa, Satoshi / Beckett, Karen / Gaugue, Isabelle / Palmer, Ruth H / Vincent, Jean-Paul

Nature cell biology

2016 Volume 18, Issue 4, Page(s) 451–457

Abstract: The apical and basolateral membranes of epithelia are insulated from each other, preventing the transfer of extracellular proteins from one side to the other. Thus, a signalling protein produced apically is not expected to reach basolateral receptors. ... ...

Abstract	The apical and basolateral membranes of epithelia are insulated from each other, preventing the transfer of extracellular proteins from one side to the other. Thus, a signalling protein produced apically is not expected to reach basolateral receptors. Evidence suggests that Wingless, the main Drosophila Wnt, is secreted apically in the embryonic epidermis. However, in the wing imaginal disc epithelium, Wingless is mostly seen on the basolateral membrane where it spreads from secreting to receiving cells. Here we examine the apico-basal movement of Wingless in Wingless-producing cells of wing imaginal discs. We find that it is presented first on the apical surface before making its way to the basolateral surface, where it is released and allowed to interact with signalling receptors. We show that Wingless transcytosis involves dynamin-dependent endocytosis from the apical surface. Subsequent trafficking from early apical endosomes to the basolateral surface requires Godzilla, a member of the RNF family of membrane-anchored E3 ubiquitin ligases. Without such transport, Wingless signalling is strongly reduced in this tissue.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/embryology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Endosomes/metabolism ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Imaginal Discs/embryology ; Imaginal Discs/metabolism ; In Situ Hybridization, Fluorescence ; Microscopy, Confocal ; RNA Interference ; Signal Transduction ; Transcytosis ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Wings, Animal/embryology ; Wings, Animal/metabolism ; Wnt1 Protein/genetics ; Wnt1 Protein/metabolism
Chemical Substances	Drosophila Proteins ; Wnt1 Protein ; wg protein, Drosophila ; Green Fluorescent Proteins (147336-22-9) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; gzl protein, Drosophila (EC 2.3.2.27)
Language	English
Publishing date	2016-03-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/ncb3325
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Article: Characterization of a thermostable carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima

Kakugawa, Satoshi / Fushinobu, Shinya / Wakagi, Takayoshi / Shoun, Hirofumi

Applied microbiology and biotechnology. 2007 Mar., v. 74, no. 3

2007

Abstract: The gene encoding carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima (tm0053) was cloned. The recombinant protein (EST53) was overexpressed in Escherichia coli without its NH₂-terminal hydrophobic region, and with a C-terminal ... ...

Abstract	The gene encoding carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima (tm0053) was cloned. The recombinant protein (EST53) was overexpressed in Escherichia coli without its NH₂-terminal hydrophobic region, and with a C-terminal hexahistidine sequence. The enzyme was purified to homogeneity by heat treatment, followed by Ni²⁺ affinity chromatography, and then characterized. Among the p-nitrophenyl esters tested, the best substrate was p-nitrophenyl decanoate with K m and k cat values of 3.1 μM and 10.8 s-¹, respectively, at 60°C and pH 7.5. The addition of O,O'-bis(2-aminoethyl)ethyleneglycol-N,N,N',N'-tetraacetic acid decreased the esterase activity, indicating that EST53 is dependent on the presence of Ca²⁺ ion. In addition, its activity was inhibited by the addition of phenylmethylsulfonyl fluoride and diethyl pyrocarbonate, indicating that it contains serine and histidine residues, which play key roles in the catalytic mechanism. EST53 shows a relatively high degree of similarity to Burkholderia lipases that belong to family I.2 of the lipolytic enzymes, whereas the local sequence around the pentapeptide of EST53 is most similar to those of Bacillus lipases belonging to family I.4.
Keywords	carboxylesterase ; triacylglycerol lipase
Language	English
Dates of publication	2007-03
Size	p. 585-591.
Publisher	Springer-Verlag
Publishing place	Berlin/Heidelberg
Document type	Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-006-0687-9
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Article: Characterization of a thermostable carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima.

Kakugawa, Satoshi / Fushinobu, Shinya / Wakagi, Takayoshi / Shoun, Hirofumi

Applied microbiology and biotechnology

2007 Volume 74, Issue 3, Page(s) 585–591

Abstract: The gene encoding carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima (tm0053) was cloned. The recombinant protein (EST53) was overexpressed in Escherichia coli without its NH(2)-terminal hydrophobic region, and with a C-terminal ... ...

Abstract	The gene encoding carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima (tm0053) was cloned. The recombinant protein (EST53) was overexpressed in Escherichia coli without its NH(2)-terminal hydrophobic region, and with a C-terminal hexahistidine sequence. The enzyme was purified to homogeneity by heat treatment, followed by Ni(2+) affinity chromatography, and then characterized. Among the p-nitrophenyl esters tested, the best substrate was p-nitrophenyl decanoate with K (m) and k (cat) values of 3.1 muM and 10.8 s(-1), respectively, at 60 degrees C and pH 7.5. The addition of O,O'-bis(2-aminoethyl)ethyleneglycol-N,N,N',N'-tetraacetic acid decreased the esterase activity, indicating that EST53 is dependent on the presence of Ca(2+) ion. In addition, its activity was inhibited by the addition of phenylmethylsulfonyl fluoride and diethyl pyrocarbonate, indicating that it contains serine and histidine residues, which play key roles in the catalytic mechanism. EST53 shows a relatively high degree of similarity to Burkholderia lipases that belong to family I.2 of the lipolytic enzymes, whereas the local sequence around the pentapeptide of EST53 is most similar to those of Bacillus lipases belonging to family I.4.
MeSH term(s)	Amino Acid Sequence ; Bacillus/genetics ; Burkholderia/genetics ; Calcium/pharmacology ; Carboxylesterase/chemistry ; Carboxylesterase/genetics ; Carboxylesterase/isolation & purification ; Carboxylesterase/metabolism ; Chemical Fractionation ; Chromatography, Affinity ; Cloning, Molecular ; Diethyl Pyrocarbonate/pharmacology ; Enzyme Activators/pharmacology ; Enzyme Inhibitors/pharmacology ; Enzyme Stability ; Escherichia coli ; Hot Temperature ; Lipase/genetics ; Molecular Sequence Data ; Phenylmethylsulfonyl Fluoride/pharmacology ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity ; Thermotoga maritima/enzymology ; Thermotoga maritima/genetics
Chemical Substances	Enzyme Activators ; Enzyme Inhibitors ; Recombinant Proteins ; Phenylmethylsulfonyl Fluoride (57KD15003I) ; Carboxylesterase (EC 3.1.1.1) ; Lipase (EC 3.1.1.3) ; Diethyl Pyrocarbonate (LMR3LZG146) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2007-03
Publishing country	Germany
Document type	Journal Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0175-7598 ; 0171-1741
ISSN (online)	1432-0614
ISSN	0175-7598 ; 0171-1741
DOI	10.1007/s00253-006-0687-9
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Article ; Online: RuvB-like protein 2 is a suppressor of influenza A virus polymerases.

Kakugawa, Satoshi / Shimojima, Masayuki / Neumann, Gabriele / Goto, Hideo / Kawaoka, Yoshihiro

Journal of virology

2009 Volume 83, Issue 13, Page(s) 6429–6434

Abstract: In pro- and eukaryotic cells, RuvB-like protein 2 (RBL2) resolves Holliday junction recombination intermediates. Here, we identified RBL2 as a suppressor of influenza A virus replication. Human RBL2 appears to interfere with the oligomerization of the ... ...

Abstract	In pro- and eukaryotic cells, RuvB-like protein 2 (RBL2) resolves Holliday junction recombination intermediates. Here, we identified RBL2 as a suppressor of influenza A virus replication. Human RBL2 appears to interfere with the oligomerization of the viral nucleoprotein, a critical step in the assembly of viral replication complexes.
MeSH term(s)	ATPases Associated with Diverse Cellular Activities ; Carrier Proteins/metabolism ; Cell Line ; DNA Helicases/metabolism ; Gene Expression Regulation, Viral ; Gene Knockdown Techniques ; Humans ; Influenza A virus/enzymology ; Influenza A virus/physiology ; Nucleocapsid Proteins ; Protein Multimerization ; RNA, Viral/metabolism ; RNA-Binding Proteins/metabolism ; RNA-Dependent RNA Polymerase/metabolism ; Viral Core Proteins/metabolism ; Virus Replication
Chemical Substances	Carrier Proteins ; NP protein, Influenza A virus ; Nucleocapsid Proteins ; RNA, Viral ; RNA-Binding Proteins ; Viral Core Proteins ; RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; DNA Helicases (EC 3.6.4.-) ; RUVBL2 protein, human (EC 3.6.4.12)
Language	English
Publishing date	2009-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00293-09
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