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Article: Rare

Oka, Akira / Hadano, Shinji / Ueda, Mahoko Takahashi / Nakagawa, So / Komaki, Gen / Ando, Tetsuya

2024 Volume 10, Issue 8, Page(s) e28643

Abstract: Eating disorders (EDs) are a type of psychiatric disorder characterized by pathological eating and related behavior and considered to be highly heritable. The purpose of this study was to explore rare variants expected to display biological functions ... ...

Abstract	Eating disorders (EDs) are a type of psychiatric disorder characterized by pathological eating and related behavior and considered to be highly heritable. The purpose of this study was to explore rare variants expected to display biological functions associated with the etiology of EDs. We performed whole exome sequencing (WES) of affected sib-pairs corresponding to disease subtype through their lifetime and their parents. From those results, rare single nucleotide variants (SNVs) concordant with sib-pairs were extracted and estimated to be most deleterious in the examined families. Two non-synonymous SNVs located on corticotropin-releasing hormone receptor 2 (
Language	English
Publishing date	2024-03-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2024.e28643
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Article ; Online: Effect of PCDH19 missense mutations on cell-to-cell proximity and neuronal development under heterotypic conditions.

Motosugi, Nami / Sugiyama, Akiko / Otomo, Asako / Sakata, Yuka / Araki, Takuma / Hadano, Shinji / Kumasaka, Natsuhiko / Fukuda, Atsushi

PNAS nexus

2024 Volume 3, Issue 3, Page(s) pgae060

Abstract: The mutation of the X-linked protocadherin (PCDH) 19 gene in heterozygous females causes epilepsy. However, because of the erosion of X-chromosome inactivation (XCI) in female human pluripotent stem cells, precise disease modeling often leads to failure. ...

Abstract	The mutation of the X-linked protocadherin (PCDH) 19 gene in heterozygous females causes epilepsy. However, because of the erosion of X-chromosome inactivation (XCI) in female human pluripotent stem cells, precise disease modeling often leads to failure. In this study, using a mathematical approach and induced pluripotent stem cells retaining XCI derived from patients with PCDH19 missense mutations, we found that heterotypic conditions, which are composed of wild-type and missense PCDH19, led to significant cell-to-cell proximity and impaired neuronal differentiation, accompanied by the aberrant accumulation of doublecortin, a microtubule-associated protein. Our findings suggest that ease of adhesion between cells expressing either wild-type or missense PCDH19 might lead to aberrant cell aggregation in early embryonic phases, causing poor neuronal development.
Language	English
Publishing date	2024-02-08
Publishing country	England
Document type	Journal Article
ISSN	2752-6542
ISSN (online)	2752-6542
DOI	10.1093/pnasnexus/pgae060
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Article ; Online: AI-based protein structure databases have the potential to accelerate rare diseases research: AlphaFoldDB and the case of IAHSP/Alsin.

Rossi Sebastiano, Matteo / Ermondi, Giuseppe / Hadano, Shinji / Caron, Giulia

Drug discovery today

2021 Volume 27, Issue 6, Page(s) 1652–1660

Abstract: Artificial intelligence (AI)-based protein structure databases are expected to have an impact on drug discovery. Here, we show how AlphaFold could support rare diseases research programs. We focus on Alsin, a protein responsible for rare motor neuron ... ...

Abstract	Artificial intelligence (AI)-based protein structure databases are expected to have an impact on drug discovery. Here, we show how AlphaFold could support rare diseases research programs. We focus on Alsin, a protein responsible for rare motor neuron diseases, such as infantile-onset ascending hereditary spastic paralysis (IAHSP) and juvenile primary lateral sclerosis (JPLS), and involved in some cases of amyotrophic lateral sclerosis (ALS). First, we compared the AlphaFoldDB human Alsin model with homology models of Alsin domains. We then evaluated the flexibility profile of Alsin and of experimentally characterized mutants present in patients with IAHSP. Next, we compared preliminary models of dimeric/tetrameric Alsin responsible for its physiological action with hypothetical models reported in the literature. Finally, we suggest the best animal model for drug candidates testing. Overall, we computationally show that drug discovery efforts toward Alsin-involving diseases should be pursued.
MeSH term(s)	Amyotrophic Lateral Sclerosis/drug therapy ; Amyotrophic Lateral Sclerosis/genetics ; Animals ; Artificial Intelligence ; Databases, Protein ; Humans ; Rare Diseases/drug therapy ; Spastic Paraplegia, Hereditary
Language	English
Publishing date	2021-12-25
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1324988-5
ISSN	1878-5832 ; 1359-6446
ISSN (online)	1878-5832
ISSN	1359-6446
DOI	10.1016/j.drudis.2021.12.018
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Article ; Online: Personalized Treatment for Infantile Ascending Hereditary Spastic Paralysis Based on In Silico Strategies.

Rossi Sebastiano, Matteo / Ermondi, Giuseppe / Sato, Kai / Otomo, Asako / Hadano, Shinji / Caron, Giulia

Molecules (Basel, Switzerland)

2022 Volume 27, Issue 20

Abstract: Infantile onset hereditary spastic paralysis (IAHSP) is a rare neurological disease diagnosed in less than 50 children worldwide. It is transmitted with a recessive pattern and originates from mutations of ... ...

Abstract	Infantile onset hereditary spastic paralysis (IAHSP) is a rare neurological disease diagnosed in less than 50 children worldwide. It is transmitted with a recessive pattern and originates from mutations of the
MeSH term(s)	Child ; Humans ; Tryptophan/genetics ; HeLa Cells ; Lysine/genetics ; Muscle Spasticity ; Precision Medicine ; Guanine Nucleotide Exchange Factors/chemistry ; Mutation ; Paralysis ; Arginine/genetics
Chemical Substances	Tryptophan (8DUH1N11BX) ; Lysine (K3Z4F929H6) ; Guanine Nucleotide Exchange Factors ; Arginine (94ZLA3W45F)
Language	English
Publishing date	2022-10-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules27207063
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Article: The N-terminal intrinsically disordered region mediates intracellular localization and self-oligomerization of ALS2

Shimakura, Kento / Sato, Kai / Mitsui, Shun / Ono, Suzuka / Otomo, Asako / Hadano, Shinji

Biochemical and biophysical research communications. 2021 Sept. 10, v. 569

2021

Abstract: ALS2, a product of the causative gene for familial amyotrophic lateral sclerosis (ALS) type 2, plays a pivotal role in the regulation of endosome dynamics by activating small GTPase Rab5 via its intrinsic guanine nucleotide-exchange factor activity. ... ...

Abstract	ALS2, a product of the causative gene for familial amyotrophic lateral sclerosis (ALS) type 2, plays a pivotal role in the regulation of endosome dynamics by activating small GTPase Rab5 via its intrinsic guanine nucleotide-exchange factor activity. Previously, we have reported that the N-terminal region of ALS2 has crucial roles in its endosomal localization and self-oligomerization, both of which are indispensable for the cellular function of ALS2. The N-terminus of ALS2 contains the regulator of chromosome condensation 1-like domain (RLD), which is predicted to form a seven-bladed β-propeller structure. Interestingly, the RLD is interrupted by the intrinsically disordered region (IDR), within which there are several amino acid residues which undergo phosphorylation. In this study, we sought to investigate as to whether and how the IDR as well as phosphorylation at either Ser483, Ser492 or Thr510 affect the intracellular localization and self-oligomerization of ALS2. All phospho- and dephospho-mimetic ALS2 mutants that were transiently expressed in HeLa cells were diffusely distributed throughout the cytosol with a partial localization to early endosomes. When expressed under Rac1-activating conditions, these mutants were localized to membrane ruffles as well as enlarged endosomes. Further, gel-filtration analysis revealed that these mutants primarily existed as a tetramer in cells. However, all these phenotypes were indistinguishable from those of wild-type ALS2. On the other hand, IDR-deleted ALS2 mutant was exclusively present in perinuclear aggregates colocalizing with the autophagy-related protein SQSTM1. Moreover, IDR-deleted ALS2 mutant formed an abnormally high molecular weight complex compared to wild-type ALS2. These results indicate that the IDR of ALS2 plays a crucial role not only in the regulation of intracellular localization but also in the self-oligomerization of ALS2 in cells, whereas phosphorylation of certain residues within the IDR exerts limited effects on such phenotypes.
Keywords	amino acids ; amyotrophic lateral sclerosis ; chromosome morphology ; cytosol ; endosomes ; gel chromatography ; genes ; guanine ; guanosinetriphosphatase ; molecular weight ; mutants ; phosphorylation ; research
Language	English
Dates of publication	2021-0910
Size	p. 106-111.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2021.06.095
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Article ; Online: The N-terminal intrinsically disordered region mediates intracellular localization and self-oligomerization of ALS2.

Shimakura, Kento / Sato, Kai / Mitsui, Shun / Ono, Suzuka / Otomo, Asako / Hadano, Shinji

Biochemical and biophysical research communications

2021 Volume 569, Page(s) 106–111

Abstract	ALS2, a product of the causative gene for familial amyotrophic lateral sclerosis (ALS) type 2, plays a pivotal role in the regulation of endosome dynamics by activating small GTPase Rab5 via its intrinsic guanine nucleotide-exchange factor activity. Previously, we have reported that the N-terminal region of ALS2 has crucial roles in its endosomal localization and self-oligomerization, both of which are indispensable for the cellular function of ALS2. The N-terminus of ALS2 contains the regulator of chromosome condensation 1-like domain (RLD), which is predicted to form a seven-bladed β-propeller structure. Interestingly, the RLD is interrupted by the intrinsically disordered region (IDR), within which there are several amino acid residues which undergo phosphorylation. In this study, we sought to investigate as to whether and how the IDR as well as phosphorylation at either Ser483, Ser492 or Thr510 affect the intracellular localization and self-oligomerization of ALS2. All phospho- and dephospho-mimetic ALS2 mutants that were transiently expressed in HeLa cells were diffusely distributed throughout the cytosol with a partial localization to early endosomes. When expressed under Rac1-activating conditions, these mutants were localized to membrane ruffles as well as enlarged endosomes. Further, gel-filtration analysis revealed that these mutants primarily existed as a tetramer in cells. However, all these phenotypes were indistinguishable from those of wild-type ALS2. On the other hand, IDR-deleted ALS2 mutant was exclusively present in perinuclear aggregates colocalizing with the autophagy-related protein SQSTM1. Moreover, IDR-deleted ALS2 mutant formed an abnormally high molecular weight complex compared to wild-type ALS2. These results indicate that the IDR of ALS2 plays a crucial role not only in the regulation of intracellular localization but also in the self-oligomerization of ALS2 in cells, whereas phosphorylation of certain residues within the IDR exerts limited effects on such phenotypes.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Blotting, Western ; Endosomes/metabolism ; Genetic Predisposition to Disease/genetics ; Guanine Nucleotide Exchange Factors/chemistry ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; HeLa Cells ; Humans ; Intracellular Space/metabolism ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/genetics ; Intrinsically Disordered Proteins/metabolism ; Microscopy, Fluorescence ; Mutation ; Phosphorylation ; Protein Binding ; Protein Multimerization ; Protein Transport ; Sequestosome-1 Protein/metabolism ; rab5 GTP-Binding Proteins/metabolism
Chemical Substances	ALS2 protein, human ; Guanine Nucleotide Exchange Factors ; Intrinsically Disordered Proteins ; SQSTM1 protein, human ; Sequestosome-1 Protein ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2021-07-06
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.2021.06.095
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Article ; Online: High-throughput quantitative analysis of axonal transport in cultured neurons from SOD1

Otomo, Asako / Ono, Suzuka / Sato, Kai / Mitsui, Shun / Shimakura, Kento / Kimura, Hiroshi / Hadano, Shinji

Neuroscience research

2021 Volume 174, Page(s) 46–52

Abstract: Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by selective loss of motor neurons. We have previously shown that autophagosome-like vesicular structures are progressively accumulated in the spinal axons of an ALS mouse ... ...

Abstract	Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by selective loss of motor neurons. We have previously shown that autophagosome-like vesicular structures are progressively accumulated in the spinal axons of an ALS mouse model, overexpressing human Cu/Zn superoxide dismutase (SOD1) mutant, prior to the onset of motor symptoms. This suggests that axonal transport perturbation can be an early sign of neuronal dysfunction. However, the exact causal relationship between axonal transport deficits and neurodegeneration is not fully understood. To clarify whether axonal transport of organelles even in neurons at early developmental stages was affected by overexpression of mutant SOD1, we conducted a microfluidic device-based high-throughput quantitative analysis of the axonal transport of acidic vesicles and mitochondria in primary cultured cortical neurons established from SOD1
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Animals ; Axonal Transport ; Disease Models, Animal ; Lab-On-A-Chip Devices ; Mice ; Mice, Transgenic ; Motor Neurons/metabolism ; Mutation/genetics ; Neurodegenerative Diseases ; Superoxide Dismutase/genetics ; Superoxide Dismutase/metabolism ; Superoxide Dismutase-1/genetics
Chemical Substances	Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2021-08-02
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	605842-5
ISSN	1872-8111 ; 0168-0102 ; 0921-8696
ISSN (online)	1872-8111
ISSN	0168-0102 ; 0921-8696
DOI	10.1016/j.neures.2021.07.005
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Article ; Online: De-erosion of X chromosome dosage compensation by the editing of

Motosugi, Nami / Sugiyama, Akiko / Okada, Chisa / Otomo, Asako / Umezawa, Akihiro / Akutsu, Hidenori / Hadano, Shinji / Fukuda, Atsushi

Cell reports methods

2022 Volume 2, Issue 12, Page(s) 100352

Abstract: Human pluripotent stem cells (hPSCs) regularly and irreversibly show the erosion of X chromosome inactivation (XCI) by long non-coding RNA (lncRNA) ...

Abstract	Human pluripotent stem cells (hPSCs) regularly and irreversibly show the erosion of X chromosome inactivation (XCI) by long non-coding RNA (lncRNA)
MeSH term(s)	Female ; Humans ; Cell Differentiation/genetics ; Dosage Compensation, Genetic ; Pluripotent Stem Cells ; X Chromosome/genetics ; X Chromosome Inactivation/genetics ; RNA, Long Noncoding/genetics
Chemical Substances	XIST non-coding RNA ; RNA, Long Noncoding
Language	English
Publishing date	2022-11-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2667-2375
ISSN (online)	2667-2375
DOI	10.1016/j.crmeth.2022.100352
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Article ; Online: Central nervous system specific high molecular weight ALS2/alsin homophilic complex is enriched in mouse brain synaptosomes.

Sato, Kai / Suzuki-Utsunomiya, Kyoko / Mitsui, Shun / Ono, Suzuka / Shimakura, Kento / Otomo, Asako / Hadano, Shinji

Biochemical and biophysical research communications

2022 Volume 638, Page(s) 168–175

Abstract: ALS2/alsin, the causative gene product for a number of juvenile recessive motor neuron diseases, acts as a guanine nucleotide exchange factor (GEF) for Rab5, regulating early endosome trafficking and maturation. It has been demonstrated that ALS2 forms a ...

Abstract	ALS2/alsin, the causative gene product for a number of juvenile recessive motor neuron diseases, acts as a guanine nucleotide exchange factor (GEF) for Rab5, regulating early endosome trafficking and maturation. It has been demonstrated that ALS2 forms a tetramer, and this oligomerization is essential for its GEF activity and endosomal localization in established cancer cells. However, despite that ALS2 deficiency is implicated in neurological diseases, neither the subcellular distribution of ALS2 nor the form of its complex in the central nervous system (CNS) has been investigated. In this study, we showed that ALS2 in the brain was enriched both in synaptosomal and cytosolic fractions, while those in the liver were almost exclusively present in cytosolic fraction by differential centrifugation. Gel filtration chromatography revealed that cytosolic ALS2 prepared both from the brain and liver formed a tetramer. Remarkably, synaptosomal ALS2 existed as a high-molecular weight complex in addition to a tetramer. Such complex was also observed not only in embryonic brain but also several neuronal and glial cultures, but not in fibroblast-derived cell lines. Thus, the high-molecular weight ALS2 complex represents a unique form of ALS2-homophilic oligomers in the CNS, which may play a role in the maintenance of neural function.
MeSH term(s)	Animals ; Mice ; Amyotrophic Lateral Sclerosis/metabolism ; Brain/metabolism ; Central Nervous System/metabolism ; Endosomes/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Molecular Weight ; Synaptosomes/metabolism
Chemical Substances	Als2 protein, mouse ; Guanine Nucleotide Exchange Factors
Language	English
Publishing date	2022-11-22
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.2022.11.061
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Article: ALS2, the small GTPase Rab17-interacting protein, regulates maturation and sorting of Rab17-associated endosomes

Ono, Suzuka / Otomo, Asako / Murakoshi, Shuji / Mitsui, Shun / Sato, Kai / Fukuda, Mitsunori / Hadano, Shinji

Biochemical and biophysical research communications. 2020 Mar. 19, v. 523, no. 4

2020

Abstract: Small GTPase Rab17 has been shown to regulate a wide range of physiological processes including cell migration in tumor cells and dendrite morphogenesis in neurons. However, molecular mechanism underlying Rab17-mediated intracellular trafficking is still ...

Abstract	Small GTPase Rab17 has been shown to regulate a wide range of physiological processes including cell migration in tumor cells and dendrite morphogenesis in neurons. However, molecular mechanism underlying Rab17-mediated intracellular trafficking is still unclear. To address this issue, we focused on Rab17-interacting protein ALS2, which was also known as a guanine nucleotide exchange factor (GEF) for Rab5, and investigated how ALS2 contributed to Rab17-associated membrane trafficking in cells. Rab17 was primarily localized to endosomal compartments, particularly to recycling endosomes, which was dependent on Rab11 expression. Upon Rac1 activation, Rab17 along with ALS2 was recruited to membrane ruffles and early endosomes in a Rab5 activity-independent manner. While RABGEF1, another Rab17-interacting Rab5 GEF, functioned as a GEF for Rab17, ALS2 did not possess such catalytic activity but merely interacted with Rab17. Importantly, ALS2 acted downstream of RABGEF1, regulating the maturation of Rab17-residing nascent endosomes to early endosome antigen 1 (EEA1)-positive early endosomes. Further, these Rab17-residing nascent endosomes were arisen via clathrin-independent endocytosis (CIE). Collectively, ALS2 plays a crucial role in the regulation of Rab17-associated endosomal trafficking and maturation, probably through their physical interaction, in cells.
Keywords	antigens ; catalytic activity ; cell movement ; endocytosis ; endosomes ; guanine nucleotide exchange factors ; guanosinetriphosphatase ; morphogenesis ; neoplasms ; research
Language	English
Dates of publication	2020-0319
Size	p. 908-915.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2019.12.122
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