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Article: Function and dysfunction of GEMIN5: understanding a novel neurodevelopmental disorder.

Nelson, Charles H / Pandey, Udai B

2024 Volume 19, Issue 11, Page(s) 2377–2386

Abstract: The recent identification of a neurodevelopmental disorder with cerebellar atrophy and motor dysfunction (NEDCAM) has resulted in an increased interest in GEMIN5, a multifunction RNA-binding protein. As the largest member of the survival motor neuron ... ...

Abstract	The recent identification of a neurodevelopmental disorder with cerebellar atrophy and motor dysfunction (NEDCAM) has resulted in an increased interest in GEMIN5, a multifunction RNA-binding protein. As the largest member of the survival motor neuron complex, GEMIN5 plays a key role in the biogenesis of small nuclear ribonucleoproteins while also exhibiting translational regulatory functions as an independent protein. Although many questions remain regarding both the pathogenesis and pathophysiology of this new disorder, considerable progress has been made in the brief time since its discovery. In this review, we examine GEMIN5 within the context of NEDCAM, focusing on the structure, function, and expression of the protein specifically in regard to the disorder itself. Additionally, we explore the current animal models of NEDCAM, as well as potential molecular pathways for treatment and future directions of study. This review provides a comprehensive overview of recent advances in our understanding of this unique member of the survival motor neuron complex.
Language	English
Publishing date	2024-01-31
Publishing country	India
Document type	Journal Article
ZDB-ID	2388460-5
ISSN	1876-7958 ; 1673-5374
ISSN (online)	1876-7958
ISSN	1673-5374
DOI	10.4103/NRR.NRR-D-23-01614
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Article ; Online: CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides against

Ortega, Juan A / Sasselli, Ivan R / Boccitto, Marco / Fleming, Andrew C / Fortuna, Tyler R / Li, Yichen / Sato, Kohei / Clemons, Tristan D / Mckenna, Elizabeth D / Nguyen, Thao P / Anderson, Eric N / Asin, Jesus / Ichida, Justin K / Pandey, Udai B / Wolin, Sandra L / Stupp, Samuel I / Kiskinis, Evangelos

Science advances

2023 Volume 9, Issue 45, Page(s) eadf7997

Abstract: Amyotrophic lateral sclerosis and frontotemporal dementia patients with a hexanucleotide repeat expansion ... ...

Abstract	Amyotrophic lateral sclerosis and frontotemporal dementia patients with a hexanucleotide repeat expansion in
MeSH term(s)	Animals ; Humans ; Frontotemporal Dementia/genetics ; Amyotrophic Lateral Sclerosis/genetics ; C9orf72 Protein/genetics ; C9orf72 Protein/metabolism ; RNA, Ribosomal/genetics ; Chromatin Immunoprecipitation Sequencing ; RNA/genetics ; Drosophila/genetics ; Drosophila/metabolism ; DNA Repeat Expansion
Chemical Substances	C9orf72 Protein ; RNA, Ribosomal ; RNA (63231-63-0)
Language	English
Publishing date	2023-11-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.adf7997
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Article ; Online: Loss of function of the ALS-associated NEK1 kinase disrupts microtubule homeostasis and nuclear import.

Mann, Jacob R / McKenna, Elizabeth D / Mawrie, Darilang / Papakis, Vasileios / Alessandrini, Francesco / Anderson, Eric N / Mayers, Ryan / Ball, Hannah E / Kaspi, Evan / Lubinski, Katherine / Baron, Desiree M / Tellez, Liana / Landers, John E / Pandey, Udai B / Kiskinis, Evangelos

Science advances

2023 Volume 9, Issue 33, Page(s) eadi5548

Abstract: Loss-of-function variants in NIMA-related kinase 1 (NEK1) constitute a major genetic cause of amyotrophic lateral sclerosis (ALS), accounting for 2 to 3% of all cases. However, ... ...

Abstract	Loss-of-function variants in NIMA-related kinase 1 (NEK1) constitute a major genetic cause of amyotrophic lateral sclerosis (ALS), accounting for 2 to 3% of all cases. However, how
MeSH term(s)	Humans ; Amyotrophic Lateral Sclerosis/genetics ; Active Transport, Cell Nucleus ; NIMA-Related Kinase 1/genetics ; Proteins ; Motor Neurons ; Microtubules ; Homeostasis
Chemical Substances	NIMA-Related Kinase 1 (EC 2.7.11.1) ; Proteins ; NEK1 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2023-08-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.adi5548
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Article ; Online: Optogenetic TDP-43 nucleation induces persistent insoluble species and progressive motor dysfunction in vivo.

Otte, Charlton G / Fortuna, Tyler R / Mann, Jacob R / Gleixner, Amanda M / Ramesh, Nandini / Pyles, Noah J / Pandey, Udai B / Donnelly, Christopher J

Neurobiology of disease

2020 Volume 146, Page(s) 105078

Abstract: TDP-43 is a predominantly nuclear DNA/RNA binding protein that is often mislocalized into insoluble cytoplasmic inclusions in post-mortem patient tissue in a variety of neurodegenerative disorders including Amyotrophic Lateral Sclerosis (ALS) and ... ...

Abstract	TDP-43 is a predominantly nuclear DNA/RNA binding protein that is often mislocalized into insoluble cytoplasmic inclusions in post-mortem patient tissue in a variety of neurodegenerative disorders including Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal dementia (FTD). The underlying causes of TDP-43 proteinopathies remain unclear, but recent studies indicate the formation of these protein assemblies is driven by aberrant phase transitions of RNA deficient TDP-43. Technical limitations have prevented our ability to understand how TDP-43 proteinopathy relates to disease pathogenesis. Current animal models of TDP-43 proteinopathy often rely on overexpression of wild-type TDP-43 to non-physiological levels that may initiate neurotoxicity through nuclear gain of function mechanisms, or by the expression of disease-causing mutations found in only a fraction of ALS patients. New technologies allowing for light-responsive control of subcellular protein crowding provide a promising approach to drive intracellular protein aggregation, as we have previously demonstrated in vitro. Here we present a model for the optogenetic induction of TDP-43 proteinopathy in Drosophila that recapitulates key features of patient pathology, including detergent insoluble cytoplamsic inclusions and progressive motor dysfunction.
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; DNA-Binding Proteins/metabolism ; Drosophila ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/pathology ; Inclusion Bodies/metabolism ; Mutation/genetics ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurons/metabolism ; Optogenetics/methods ; TDP-43 Proteinopathies/genetics
Chemical Substances	DNA-Binding Proteins
Language	English
Publishing date	2020-09-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2020.105078
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Article ; Online: Antagonistic effect of cyclin-dependent kinases and a calcium-dependent phosphatase on polyglutamine-expanded androgen receptor toxic gain of function.

Science advances

2023 Volume 9, Issue 1, Page(s) eade1694

Abstract: Spinal and bulbar muscular atrophy is caused by polyglutamine (polyQ) expansions in androgen receptor (AR), generating gain-of-function toxicity that may involve phosphorylation. Using cellular and animal models, we investigated what kinases and ... ...

Abstract	Spinal and bulbar muscular atrophy is caused by polyglutamine (polyQ) expansions in androgen receptor (AR), generating gain-of-function toxicity that may involve phosphorylation. Using cellular and animal models, we investigated what kinases and phosphatases target polyQ-expanded AR, whether polyQ expansions modify AR phosphorylation, and how this contributes to neurodegeneration. Mass spectrometry showed that polyQ expansions preserve native phosphorylation and increase phosphorylation at conserved sites controlling AR stability and transactivation. In small-molecule screening, we identified that CDC25/CDK2 signaling could enhance AR phosphorylation, and the calcium-sensitive phosphatase calcineurin had opposite effects. Pharmacologic and genetic manipulation of these kinases and phosphatases modified polyQ-expanded AR function and toxicity in cells, flies, and mice. Ablation of CDK2 reduced AR phosphorylation in the brainstem and restored expression of
MeSH term(s)	Mice ; Animals ; Receptors, Androgen/chemistry ; Calcium ; Gain of Function Mutation ; Cyclin-Dependent Kinases/genetics ; Phosphoric Monoester Hydrolases/genetics
Chemical Substances	polyglutamine (26700-71-0) ; Receptors, Androgen ; Calcium (SY7Q814VUP) ; Cyclin-Dependent Kinases (EC 2.7.11.22) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
Language	English
Publishing date	2023-01-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.ade1694
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Article ; Online: Methods to assay Drosophila behavior.

Nichols, Charles D / Becnel, Jaime / Pandey, Udai B

Journal of visualized experiments : JoVE

2012 , Issue 61

Abstract: Drosophila melanogaster, the fruit fly, has been used to study molecular mechanisms of a wide range of human diseases such as cancer, cardiovascular disease and various neurological diseases(1). We have optimized simple and robust behavioral assays for ... ...

Abstract	Drosophila melanogaster, the fruit fly, has been used to study molecular mechanisms of a wide range of human diseases such as cancer, cardiovascular disease and various neurological diseases(1). We have optimized simple and robust behavioral assays for determining larval locomotion, adult climbing ability (RING assay), and courtship behaviors of Drosophila. These behavioral assays are widely applicable for studying the role of genetic and environmental factors on fly behavior. Larval crawling ability can be reliably used for determining early stage changes in the crawling abilities of Drosophila larvae and also for examining effect of drugs or human disease genes (in transgenic flies) on their locomotion. The larval crawling assay becomes more applicable if expression or abolition of a gene causes lethality in pupal or adult stages, as these flies do not survive to adulthood where they otherwise could be assessed. This basic assay can also be used in conjunction with bright light or stress to examine additional behavioral responses in Drosophila larvae. Courtship behavior has been widely used to investigate genetic basis of sexual behavior, and can also be used to examine activity and coordination, as well as learning and memory. Drosophila courtship behavior involves the exchange of various sensory stimuli including visual, auditory, and chemosensory signals between males and females that lead to a complex series of well characterized motor behaviors culminating in successful copulation. Traditional adult climbing assays (negative geotaxis) are tedious, labor intensive, and time consuming, with significant variation between different trials(2-4). The rapid iterative negative geotaxis (RING) assay(5) has many advantages over more widely employed protocols, providing a reproducible, sensitive, and high throughput approach to quantify adult locomotor and negative geotaxis behaviors. In the RING assay, several genotypes or drug treatments can be tested simultaneously using large number of animals, with the high-throughput approach making it more amenable for screening experiments.
MeSH term(s)	Animals ; Behavior, Animal ; Drosophila melanogaster/physiology ; Female ; Locomotion ; Male
Language	English
Publishing date	2012-03-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/3795
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Article: Methods to assay Drosophila behavior

Nichols, Charles D / Becnel, Jaime / Pandey, Udai B

Journal of visualized experiments. 2012 Mar. 07, , no. 61

2012

Abstract: Drosophila melanogaster, the fruit fly, has been used to study molecular mechanisms of a wide range of human diseases such as cancer, cardiovascular disease and various neurological diseases1. We have optimized simple and robust behavioral assays for ... ...

Abstract	Drosophila melanogaster, the fruit fly, has been used to study molecular mechanisms of a wide range of human diseases such as cancer, cardiovascular disease and various neurological diseases1. We have optimized simple and robust behavioral assays for determining larval locomotion, adult climbing ability (RING assay), and courtship behaviors of Drosophila. These behavioral assays are widely applicable for studying the role of genetic and environmental factors on fly behavior. Larval crawling ability can be reliably used for determining early stage changes in the crawling abilities of Drosophila larvae and also for examining effect of drugs or human disease genes (in transgenic flies) on their locomotion. The larval crawling assay becomes more applicable if expression or abolition of a gene causes lethality in pupal or adult stages, as these flies do not survive to adulthood where they otherwise could be assessed. This basic assay can also be used in conjunction with bright light or stress to examine additional behavioral responses in Drosophila larvae. Courtship behavior has been widely used to investigate genetic basis of sexual behavior, and can also be used to examine activity and coordination, as well as learning and memory. Drosophila courtship behavior involves the exchange of various sensory stimuli including visual, auditory, and chemosensory signals between males and females that lead to a complex series of well characterized motor behaviors culminating in successful copulation. Traditional adult climbing assays (negative geotaxis) are tedious, labor intensive, and time consuming, with significant variation between different trials2-4. The rapid iterative negative geotaxis (RING) assay5 has many advantages over more widely employed protocols, providing a reproducible, sensitive, and high throughput approach to quantify adult locomotor and negative geotaxis behaviors. In the RING assay, several genotypes or drug treatments can be tested simultaneously using large number of animals, with the high-throughput approach making it more amenable for screening experiments.
Keywords	Drosophila melanogaster ; adulthood ; copulation ; courtship ; death ; females ; fruit flies ; genes ; genotype ; geotaxis ; imagos ; insect behavior ; labor ; larvae ; locomotion ; males ; memory ; pupae ; screening ; transgenic insects
Language	English
Dates of publication	2012-0307
Size	p. e3795.
Publishing place	Journal of Visualized Experiments
Document type	Article
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/3795
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Article ; Online: Huntingtin-mediated axonal transport requires arginine methylation by PRMT6.

Migazzi, Alice / Scaramuzzino, Chiara / Anderson, Eric N / Tripathy, Debasmita / Hernández, Ivó H / Grant, Rogan A / Roccuzzo, Michela / Tosatto, Laura / Virlogeux, Amandine / Zuccato, Chiara / Caricasole, Andrea / Ratovitski, Tamara / Ross, Christopher A / Pandey, Udai B / Lucas, José J / Saudou, Frédéric / Pennuto, Maria / Basso, Manuela

Cell reports

2021 Volume 35, Issue 2, Page(s) 108980

Abstract: The huntingtin (HTT) protein transports various organelles, including vesicles containing neurotrophic factors, from embryonic development throughout life. To better understand how HTT mediates axonal transport and why this function is disrupted in ... ...

Abstract	The huntingtin (HTT) protein transports various organelles, including vesicles containing neurotrophic factors, from embryonic development throughout life. To better understand how HTT mediates axonal transport and why this function is disrupted in Huntington's disease (HD), we study vesicle-associated HTT and find that it is dimethylated at a highly conserved arginine residue (R118) by the protein arginine methyltransferase 6 (PRMT6). Without R118 methylation, HTT associates less with vesicles, anterograde trafficking is diminished, and neuronal death ensues-very similar to what occurs in HD. Inhibiting PRMT6 in HD cells and neurons exacerbates mutant HTT (mHTT) toxicity and impairs axonal trafficking, whereas overexpressing PRMT6 restores axonal transport and neuronal viability, except in the presence of a methylation-defective variant of mHTT. In HD flies, overexpressing PRMT6 rescues axonal defects and eclosion. Arginine methylation thus regulates HTT-mediated vesicular transport along the axon, and increasing HTT methylation could be of therapeutic interest for HD.
MeSH term(s)	Amino Acid Sequence ; Animals ; Arginine/metabolism ; Axonal Transport/genetics ; Brain-Derived Neurotrophic Factor/genetics ; Brain-Derived Neurotrophic Factor/metabolism ; Cell Death ; Disease Models, Animal ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Epigenesis, Genetic ; Genes, Reporter ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Humans ; Huntingtin Protein/genetics ; Huntingtin Protein/metabolism ; Huntington Disease/genetics ; Huntington Disease/metabolism ; Huntington Disease/pathology ; Methylation ; Mice ; Mice, Transgenic ; Neuromuscular Junction/genetics ; Neuromuscular Junction/metabolism ; Neuromuscular Junction/pathology ; Neurons/metabolism ; Neurons/pathology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein-Arginine N-Methyltransferases/genetics ; Protein-Arginine N-Methyltransferases/metabolism ; Transport Vesicles/genetics ; Transport Vesicles/metabolism ; Transport Vesicles/pathology
Chemical Substances	Brain-Derived Neurotrophic Factor ; HTT protein, human ; Huntingtin Protein ; Nuclear Proteins ; Protein Isoforms ; enhanced green fluorescent protein ; Green Fluorescent Proteins (147336-22-9) ; BDNF protein, human (7171WSG8A2) ; Arginine (94ZLA3W45F) ; PRMT6 protein, human (EC 2.1.1.319) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319)
Language	English
Publishing date	2021-05-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.108980
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Article ; Online: NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility.

Gleixner, Amanda M / Verdone, Brandie Morris / Otte, Charlton G / Anderson, Eric N / Ramesh, Nandini / Shapiro, Olivia R / Gale, Jenna R / Mauna, Jocelyn C / Mann, Jacob R / Copley, Katie E / Daley, Elizabeth L / Ortega, Juan A / Cicardi, Maria Elena / Kiskinis, Evangelos / Kofler, Julia / Pandey, Udai B / Trotti, Davide / Donnelly, Christopher J

Nature communications

2022 Volume 13, Issue 1, Page(s) 3380

Abstract: A G4C2 hexanucleotide repeat expansion in the C9orf72 gene is the most common genetic cause of ALS and FTLD (C9-ALS/FTLD) with cytoplasmic TDP-43 inclusions observed in regions of neurodegeneration. The accumulation of repetitive RNAs and dipeptide ... ...

Abstract	A G4C2 hexanucleotide repeat expansion in the C9orf72 gene is the most common genetic cause of ALS and FTLD (C9-ALS/FTLD) with cytoplasmic TDP-43 inclusions observed in regions of neurodegeneration. The accumulation of repetitive RNAs and dipeptide repeat protein (DPR) are two proposed mechanisms of toxicity in C9-ALS/FTLD and linked to impaired nucleocytoplasmic transport. Nucleocytoplasmic transport is regulated by the phenylalanine-glycine nucleoporins (FG nups) that comprise the nuclear pore complex (NPC) permeability barrier. However, the relationship between FG nups and TDP-43 pathology remains elusive. Our studies show that nuclear depletion and cytoplasmic mislocalization of one FG nup, NUP62, is linked to TDP-43 mislocalization in C9-ALS/FTLD iPSC neurons. Poly-glycine arginine (GR) DPR accumulation initiates the formation of cytoplasmic RNA granules that recruit NUP62 and TDP-43. Cytoplasmic NUP62 and TDP-43 interactions promotes their insolubility and NUP62:TDP-43 inclusions are frequently found in C9orf72 ALS/FTLD as well as sporadic ALS/FTLD postmortem CNS tissue. Our findings indicate NUP62 cytoplasmic mislocalization contributes to TDP-43 proteinopathy in ALS/FTLD.
MeSH term(s)	Amyotrophic Lateral Sclerosis/metabolism ; C9orf72 Protein/genetics ; DNA Repeat Expansion ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Dipeptides/metabolism ; Frontotemporal Lobar Degeneration/metabolism ; Glycine/genetics ; Humans
Chemical Substances	C9orf72 Protein ; DNA-Binding Proteins ; Dipeptides ; Glycine (TE7660XO1C)
Language	English
Publishing date	2022-06-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-31098-6
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Article ; Online: Pathogenic variants of Valosin-containing protein induce lysosomal damage and transcriptional activation of autophagy regulators in neuronal cells.

Neuropathology and applied neurobiology

2022 Volume 48, Issue 5, Page(s) e12818

Abstract: Aim: Mutations in the valosin-containing protein (VCP) gene cause various lethal proteinopathies that mainly include inclusion body myopathy with Paget's disease of bone and frontotemporal dementia (IBMPFD) and amyotrophic lateral sclerosis (ALS). ... ...

Abstract	Aim: Mutations in the valosin-containing protein (VCP) gene cause various lethal proteinopathies that mainly include inclusion body myopathy with Paget's disease of bone and frontotemporal dementia (IBMPFD) and amyotrophic lateral sclerosis (ALS). Different pathological mechanisms have been proposed. Here, we define the impact of VCP mutants on lysosomes and how cellular homeostasis is restored by inducing autophagy in the presence of lysosomal damage. Methods: By electron microscopy, we studied lysosomal morphology in VCP animal and motoneuronal models. With the use of western blotting, real-time quantitative polymerase chain reaction (RT-qPCR), immunofluorescence and filter trap assay, we evaluated the effect of selected VCP mutants in neuronal cells on lysosome size and activity, lysosomal membrane permeabilization and their impact on autophagy. Results: We found that VCP mutants induce the formation of aberrant multilamellar organelles in VCP animal and cell models similar to those found in patients with VCP mutations or with lysosomal storage disorders. In neuronal cells, we found altered lysosomal activity characterised by membrane permeabilization with galectin-3 redistribution and activation of PPP3CB. This selectively activated the autophagy/lysosomal transcriptional regulator TFE3, but not TFEB, and enhanced both SQSTM1/p62 and lipidated MAP1LC3B levels inducing autophagy. Moreover, we found that wild type VCP, but not the mutants, counteracted lysosomal damage induced either by trehalose or by a mutant form of SOD1 (G93A), also blocking the formation of its insoluble intracellular aggregates. Thus, chronic activation of autophagy might fuel the formation of multilamellar bodies. Conclusion: Together, our findings provide insights into the pathogenesis of VCP-related diseases, by proposing a novel mechanism of multilamellar body formation induced by VCP mutants that involves lysosomal damage and induction of lysophagy.
MeSH term(s)	Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Animals ; Autophagy/genetics ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Lysosomes/metabolism ; Motor Neurons/metabolism ; Transcriptional Activation ; Valosin Containing Protein/genetics ; Valosin Containing Protein/metabolism
Chemical Substances	Cell Cycle Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; Valosin Containing Protein (EC 3.6.4.6)
Language	English
Publishing date	2022-05-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80371-6
ISSN	1365-2990 ; 0305-1846
ISSN (online)	1365-2990
ISSN	0305-1846
DOI	10.1111/nan.12818
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