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Article ; Online: Scrambling the genome in cancer: causes and consequences of complex chromosome rearrangements.

Krupina, Ksenia / Goginashvili, Alexander / Cleveland, Don W

2023 Volume 25, Issue 3, Page(s) 196–210

Abstract: Complex chromosome rearrangements, known as chromoanagenesis, are widespread in cancer. Based on large-scale DNA sequencing of human tumours, the most frequent type of complex chromosome rearrangement is chromothripsis, a massive, localized and clustered ...

Abstract	Complex chromosome rearrangements, known as chromoanagenesis, are widespread in cancer. Based on large-scale DNA sequencing of human tumours, the most frequent type of complex chromosome rearrangement is chromothripsis, a massive, localized and clustered rearrangement of one (or a few) chromosomes seemingly acquired in a single event. Chromothripsis can be initiated by mitotic errors that produce a micronucleus encapsulating a single chromosome or chromosomal fragment. Rupture of the unstable micronuclear envelope exposes its chromatin to cytosolic nucleases and induces chromothriptic shattering. Found in up to half of tumours included in pan-cancer genomic analyses, chromothriptic rearrangements can contribute to tumorigenesis through inactivation of tumour suppressor genes, activation of proto-oncogenes, or gene amplification through the production of self-propagating extrachromosomal circular DNAs encoding oncogenes or genes conferring anticancer drug resistance. Here, we discuss what has been learned about the mechanisms that enable these complex genomic rearrangements and their consequences in cancer.
MeSH term(s)	Humans ; Chromothripsis ; Chromatin ; DNA/genetics ; Cell Nucleus ; Neoplasms/genetics ; Gene Rearrangement ; Chromosome Aberrations
Chemical Substances	Chromatin ; DNA (9007-49-2)
Language	English
Publishing date	2023-11-08
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2035157-4
ISSN	1471-0064 ; 1471-0056
ISSN (online)	1471-0064
ISSN	1471-0056
DOI	10.1038/s41576-023-00663-0
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Zs.MG 40: Show issues

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Article ; Online: Causes and consequences of micronuclei.

Krupina, Ksenia / Goginashvili, Alexander / Cleveland, Don W

Current opinion in cell biology

2021 Volume 70, Page(s) 91–99

Abstract: Micronuclei are small membrane-bounded compartments with a DNA content encapsulated by a nuclear envelope and spatially separated from the primary nucleus. Micronuclei have long been linked to chromosome instability, genome rearrangements, and ... ...

Abstract	Micronuclei are small membrane-bounded compartments with a DNA content encapsulated by a nuclear envelope and spatially separated from the primary nucleus. Micronuclei have long been linked to chromosome instability, genome rearrangements, and mutagenesis. They are frequently found in cancers, during senescence, and after genotoxic stress. Compromised integrity of the micronuclear envelope delays or disrupts DNA replication, inhibits DNA repair, and exposes micronuclear DNA directly to cytoplasm. Micronuclei play a central role in tumorigenesis, with micronuclear DNA being a source of complex genome rearrangements (including chromothripsis) and promoting a cyclic GMP-AMP synthase (cGAS)-mediated cellular immune response that may contribute to cancer metastasis. Here, we discuss recent findings on how micronuclei are generated, what the consequences are, and what cellular mechanisms can be applied to protect against micronucleation.
MeSH term(s)	Chromothripsis ; DNA Damage ; Genomic Instability ; Humans ; Micronuclei, Chromosome-Defective ; Nuclear Envelope
Language	English
Publishing date	2021-02-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2021.01.004
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Zs.A 2963: Show issues

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Book ; Online: Novel Mechanism of Fasting Response in Pancreatic β Cells

Goginashvili, Alexander

2014

Abstract: Diss., Eidgenössische Technische Hochschule ETH Zürich, Nr. 21906, ... ...

Abstract	Diss., Eidgenössische Technische Hochschule ETH Zürich, Nr. 21906, 2014
Keywords	BAUCHSPEICHELDRÜSE (ANATOMIE UND PHYSIOLOGIE) ; PHYSIOLOGIE VON ZELLE UND ORGANISMUS ; INSULIN (HORMONE) ; GRANULA + EINSCHLUSSKÖRPERCHEN (CYTOLOGIE) ; LYSOSOMEN (CYTOLOGIE) ; REGULATION UND STEUERUNG DURCH ENZYME (BIOCHEMIE) ; DIABETES MELLITUS + HYPOINSULINISMUS (PATHOLOGIE)
Language	English
Publisher	Zürich, ETH-Zürich
Publishing country	ch
Document type	Book ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Thesis ; Online: Novel Mechanism of Fasting Response in Pancreatic β Cells

Goginashvili, Alexander

2014

Keywords	BAUCHSPEICHELDRÜSE (ANATOMIE UND PHYSIOLOGIE) ; PHYSIOLOGIE VON ZELLE UND ORGANISMUS ; INSULIN (HORMONE) ; GRANULA + EINSCHLUSSKÖRPERCHEN (CYTOLOGIE) ; LYSOSOMEN (CYTOLOGIE) ; REGULATION UND STEUERUNG DURCH ENZYME (BIOCHEMIE) ; DIABETES MELLITUS + HYPOINSULINISMUS (PATHOLOGIE) ; PANCREAS (ANATOMY AND PHYSIOLOGY) ; PHYSIOLOGY OF THE CELL AND THE ORGANISM ; INSULIN (HORMONES) ; GRANULA + ENCLOSED BODIES (CYTOLOGY) ; LYSOSOMES (CYTOLOGY) ; REGULATION AND CONTROL BY ENZYMES (BIOCHEMISTRY) ; DIABETES MELLITUS + HYPOINSULINISM (PATHOLOGY) ; info:eu-repo/classification/ddc/610 ; info:eu-repo/classification/ddc/570 ; Medical sciences ; medicine ; Life sciences
Language	English
Publisher	ETH Zurich
Publishing country	ch
Document type	Thesis ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Breaking Bad and Breaking Good: β-Cell Autophagy Pathways in Diabetes.

Vivot, Kevin / Pasquier, Adrien / Goginashvili, Alexander / Ricci, Romeo

Journal of molecular biology

2019 Volume 432, Issue 5, Page(s) 1494–1513

Abstract: For many decades the lysosome has been recognized as the terminal center of cellular waste disposal. Products of lysosomal degradation are either recycled in biosynthetic pathways or are further metabolized to produce energy. As such the lysosome was ... ...

Abstract	For many decades the lysosome has been recognized as the terminal center of cellular waste disposal. Products of lysosomal degradation are either recycled in biosynthetic pathways or are further metabolized to produce energy. As such the lysosome was attributed a rather passive role in cellular metabolism merely transforming bulk material into small metabolites. More recently, however, the emerging evidence has brought the lysosome to the center of nutrient sensing as the organelle that harbors a complex signaling machinery which dynamically and actively regulates cell metabolism. The pancreatic β cell is unique in as much as nutrient sensing is directly coupled to insulin secretion. Importantly, defects in insulin secretion constitute a hallmark in the progression of patients from a state of impaired glucose tolerance to full blown type 2 diabetes (T2D). However, mechanisms linking nutrient-dependent lysosomal function to insulin secretion and more generally to β cell health have evolved only very recently. This review discusses emerging concepts in macroautophagy and macroautophagy-independent processes of cargo delivery to lysosomes as well as nutrient-dependent lysosomal signaling specifically in the context of β cell function in health and disease. Such mechanisms may provide a novel source of therapeutic targets to be exploited in the context of β cell failure in diabetes in the near future.
MeSH term(s)	Animals ; Autophagy/physiology ; Diabetes Mellitus, Type 2/metabolism ; Humans ; Hydrolases/metabolism ; Insulin/biosynthesis ; Insulin/metabolism ; Insulin-Secreting Cells/metabolism ; Lysosomes/metabolism ; Nutrients/metabolism ; Protein Transport ; Signal Transduction
Chemical Substances	Insulin ; Hydrolases (EC 3.-)
Language	English
Publishing date	2019-08-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2019.07.030
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Zs.A 867: Show issues

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Article: Breaking Bad and Breaking Good: β-Cell Autophagy Pathways in Diabetes

Vivot, Kevin / Pasquier, Adrien / Goginashvili, Alexander / Ricci, Romeo

Elsevier Ltd Journal of molecular biology. 2019 July 19,

2019

Abstract	For many decades the lysosome has been recognized as the terminal center of cellular waste disposal. Products of lysosomal degradation are either recycled in biosynthetic pathways or are further metabolized to produce energy. As such the lysosome was attributed a rather passive role in cellular metabolism merely transforming bulk material into small metabolites. More recently, however, the emerging evidence has brought the lysosome to the center of nutrient sensing as the organelle that harbors a complex signaling machinery which dynamically and actively regulates cell metabolism.The pancreatic β cell is unique in as much as nutrient sensing is directly coupled to insulin secretion. Importantly, defects in insulin secretion constitute a hallmark in the progression of patients from a state of impaired glucose tolerance to full blown type 2 diabetes (T2D). However, mechanisms linking nutrient-dependent lysosomal function to insulin secretion and more generally to β cell health have evolved only very recently. This review discusses emerging concepts in macroautophagy and macroautophagy-independent processes of cargo delivery to lysosomes as well as nutrient-dependent lysosomal signaling specifically in the context of β cell function in health and disease. Such mechanisms may provide a novel source of therapeutic targets to be exploited in the context of β cell failure in diabetes in the near future.
Keywords	autophagy ; biochemical pathways ; energy ; glucose tolerance ; insulin secretion ; islets of Langerhans ; lysosomes ; metabolites ; noninsulin-dependent diabetes mellitus ; patients ; therapeutics ; waste disposal
Language	English
Dates of publication	2019-0719
Publishing place	Elsevier Ltd
Document type	Article
Note	Pre-press version
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2019.07.030
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Lysosomes in nutrient signalling: A focus on pancreatic β-cells.

Mészáros, Gergő / Pasquier, Adrien / Vivot, Kevin / Goginashvili, Alexander / Ricci, Romeo

Diabetes, obesity & metabolism

2018 Volume 20 Suppl 2, Page(s) 104–115

Abstract: Regulated insulin secretion from pancreatic β-cells is a major process maintaining glucose homeostasis in mammals. Enhancing insulin release in response to chronic nutrient overload and obesity-related insulin resistance (pre-diabetes) requires several ... ...

Abstract	Regulated insulin secretion from pancreatic β-cells is a major process maintaining glucose homeostasis in mammals. Enhancing insulin release in response to chronic nutrient overload and obesity-related insulin resistance (pre-diabetes) requires several adaptive cellular mechanisms maintaining β-cell health under such stresses. Once these mechanisms are overwhelmed, β-cell failure occurs leading to full-blown Type 2 Diabetes (T2D). Nutrient-dependent macroautophagy represents one such adaptive mechanism in β-cells. While macroautophagy levels are high and protective in β-cells in pre-diabetes, they decrease at later stages contributing to β-cell failure. However, mechanisms compromising macroautophagy in β-cells remain poorly understood. In this review, we discuss how recently discovered signalling cascades that emanate from the limiting membrane of lysosomes contribute to changes in macroautophagy flux in physiology and disease. In particular, these mechanisms are put into context with β-cell function highlighting most recently described links between nutrient-dependent lysosomal signalling pathways and insulin secretion. Understanding these mechanisms in response to metabolic stress might pave the way for development of more tailored treatment strategies aimed at preserving β-cell health.
MeSH term(s)	Autophagy/physiology ; Diabetes Mellitus, Type 2/physiopathology ; Energy Metabolism/physiology ; Humans ; Insulin/metabolism ; Insulin Secretion/physiology ; Insulin-Secreting Cells/physiology ; Intracellular Membranes/enzymology ; Lysosomes/physiology ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Nutrients/metabolism ; Protein Kinases/metabolism ; Signal Transduction/physiology
Chemical Substances	Insulin ; Nutrients ; Protein Kinases (EC 2.7.-) ; AMP-activated protein kinase kinase (EC 2.7.1.-) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
Language	English
Publishing date	2018-09-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1454944-x
ISSN	1463-1326 ; 1462-8902
ISSN (online)	1463-1326
ISSN	1462-8902
DOI	10.1111/dom.13389
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Zs.A 5442: Show issues

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Article ; Online: Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition.

Lu, Shan / Hu, Jiaojiao / Arogundade, Olubankole Aladesuyi / Goginashvili, Alexander / Vazquez-Sanchez, Sonia / Diedrich, Jolene K / Gu, Jinge / Blum, Jacob / Oung, Spencer / Ye, Qiaozhen / Yu, Haiyang / Ravits, John / Liu, Cong / Yates, John R / Cleveland, Don W

Nature cell biology

2022 Volume 24, Issue 9, Page(s) 1378–1393

Abstract: While acetylated, RNA-binding-deficient TDP-43 reversibly phase separates within nuclei into complex droplets (anisosomes) comprised of TDP-43-containing liquid outer shells and liquid centres of HSP70-family chaperones, cytoplasmic aggregates of TDP-43 ... ...

Abstract	While acetylated, RNA-binding-deficient TDP-43 reversibly phase separates within nuclei into complex droplets (anisosomes) comprised of TDP-43-containing liquid outer shells and liquid centres of HSP70-family chaperones, cytoplasmic aggregates of TDP-43 are hallmarks of multiple neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS). Here we show that transient oxidative stress, proteasome inhibition or inhibition of the ATP-dependent chaperone activity of HSP70 provokes reversible cytoplasmic TDP-43 de-mixing and transition from liquid to gel/solid, independently of RNA binding or stress granules. Isotope labelling mass spectrometry was used to identify that phase-separated cytoplasmic TDP-43 is bound by the small heat-shock protein HSPB1. Binding is direct, mediated through TDP-43's RNA binding and low-complexity domains. HSPB1 partitions into TDP-43 droplets, inhibits TDP-43 assembly into fibrils, and is essential for disassembly of stress-induced TDP-43 droplets. A decrease in HSPB1 promotes cytoplasmic TDP-43 de-mixing and mislocalization. HSPB1 depletion was identified in spinal motor neurons of patients with ALS containing aggregated TDP-43. These findings identify HSPB1 to be a regulator of cytoplasmic TDP-43 phase separation and aggregation.
MeSH term(s)	Adenosine Triphosphate ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Heat-Shock Proteins, Small ; Humans ; Molecular Chaperones/genetics ; Phase Transition ; Proteasome Endopeptidase Complex ; RNA/metabolism
Chemical Substances	DNA-Binding Proteins ; HSP70 Heat-Shock Proteins ; HSPB1 protein, human ; Heat-Shock Proteins ; Heat-Shock Proteins, Small ; Molecular Chaperones ; RNA (63231-63-0) ; Adenosine Triphosphate (8L70Q75FXE) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2022-09-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-022-00988-8
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Lysosomal degradation of newly formed insulin granules contributes to β cell failure in diabetes.

Nature communications

2019 Volume 10, Issue 1, Page(s) 3312

Abstract: Compromised function of insulin-secreting pancreatic β cells is central to the development and progression of Type 2 Diabetes (T2D). However, the mechanisms underlying β cell failure remain incompletely understood. Here, we report that metabolic stress ... ...

Abstract	Compromised function of insulin-secreting pancreatic β cells is central to the development and progression of Type 2 Diabetes (T2D). However, the mechanisms underlying β cell failure remain incompletely understood. Here, we report that metabolic stress markedly enhances macroautophagy-independent lysosomal degradation of nascent insulin granules. In different model systems of diabetes including of human origin, stress-induced nascent granule degradation (SINGD) contributes to loss of insulin along with mammalian/mechanistic Target of Rapamycin (mTOR)-dependent suppression of macroautophagy. Expression of Protein Kinase D (PKD), a negative regulator of SINGD, is reduced in diabetic β cells. Pharmacological activation of PKD counters SINGD and delays the onset of T2D. Conversely, inhibition of PKD exacerbates SINGD, mitigates insulin secretion and accelerates diabetes. Finally, reduced levels of lysosomal tetraspanin CD63 prevent SINGD, leading to increased insulin secretion. Overall, our findings implicate aberrant SINGD in the pathogenesis of diabetes and suggest new therapeutic strategies to prevent β cell failure.
MeSH term(s)	Animals ; Diabetes Mellitus, Type 2/genetics ; Diabetes Mellitus, Type 2/metabolism ; Diabetes Mellitus, Type 2/physiopathology ; Humans ; Insulin/chemistry ; Insulin/metabolism ; Insulin Secretion ; Insulin-Secreting Cells/cytology ; Insulin-Secreting Cells/metabolism ; Lysosomes/metabolism ; Macroautophagy ; Male ; Mice, Inbred C57BL ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; TOR Serine-Threonine Kinases/genetics ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	Insulin ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; protein kinase D (EC 2.7.10.-) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2019-07-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-019-11170-4
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Article ; Online: Polyglutamine-Expanded Huntingtin Exacerbates Age-Related Disruption of Nuclear Integrity and Nucleocytoplasmic Transport.

Gasset-Rosa, Fatima / Chillon-Marinas, Carlos / Goginashvili, Alexander / Atwal, Ranjit Singh / Artates, Jonathan W / Tabet, Ricardos / Wheeler, Vanessa C / Bang, Anne G / Cleveland, Don W / Lagier-Tourenne, Clotilde

Neuron

2017 Volume 94, Issue 1, Page(s) 48–57.e4

Abstract: Onset of neurodegenerative disorders, including Huntington's disease, is strongly influenced by aging. Hallmarks of aged cells include compromised nuclear envelope integrity, impaired nucleocytoplasmic transport, and accumulation of DNA double-strand ... ...

Abstract	Onset of neurodegenerative disorders, including Huntington's disease, is strongly influenced by aging. Hallmarks of aged cells include compromised nuclear envelope integrity, impaired nucleocytoplasmic transport, and accumulation of DNA double-strand breaks. We show that mutant huntingtin markedly accelerates all of these cellular phenotypes in a dose- and age-dependent manner in cortex and striatum of mice. Huntingtin-linked polyglutamine initially accumulates in nuclei, leading to disruption of nuclear envelope architecture, partial sequestration of factors essential for nucleocytoplasmic transport (Gle1 and RanGAP1), and intranuclear accumulation of mRNA. In aged mice, accumulation of RanGAP1 together with polyglutamine is shifted to perinuclear and cytoplasmic areas. Consistent with findings in mice, marked alterations in nuclear envelope morphology, abnormal localization of RanGAP1, and nuclear accumulation of mRNA were found in cortex of Huntington's disease patients. Overall, our findings identify polyglutamine-dependent inhibition of nucleocytoplasmic transport and alteration of nuclear integrity as a central component of Huntington's disease.
MeSH term(s)	Active Transport, Cell Nucleus ; Adult ; Aged, 80 and over ; Aging/metabolism ; Animals ; Case-Control Studies ; Cell Nucleus ; Cerebral Cortex/metabolism ; Female ; GTPase-Activating Proteins/metabolism ; Humans ; Huntingtin Protein/metabolism ; Male ; Mice ; Middle Aged ; Mutation ; Neostriatum/metabolism ; Nuclear Envelope/metabolism ; Nucleocytoplasmic Transport Proteins/metabolism ; Peptides/metabolism ; RNA, Messenger/metabolism ; Young Adult
Chemical Substances	GTPase-Activating Proteins ; Gle1 protein, human ; Gle1 protein, mouse ; HTT protein, human ; Htt protein, mouse ; Huntingtin Protein ; Nucleocytoplasmic Transport Proteins ; Peptides ; RANGAP1 protein, human ; RNA, Messenger ; Rangap1 protein, mouse ; polyglutamine (26700-71-0)
Language	English
Publishing date	2017-04-05
Publishing country	United States
Document type	Journal Article ; Video-Audio Media
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2017.03.027
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