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Article ; Online: Mitochondrial calcium signaling in non-neuronal cells: Implications for Alzheimer's disease pathogenesis.

Raghav, Darpan / Shukla, Shatakshi / Jadiya, Pooja

Biochimica et biophysica acta. Molecular basis of disease

2024 Volume 1870, Issue 5, Page(s) 167169

Abstract: Mitochondrial dysregulation is pivotal in Alzheimer's disease (AD) pathogenesis. Calcium governs vital mitochondrial processes impacting energy conversion, oxidative stress, and cell death signaling. Disruptions in mitochondrial calcium ( ...

Abstract	Mitochondrial dysregulation is pivotal in Alzheimer's disease (AD) pathogenesis. Calcium governs vital mitochondrial processes impacting energy conversion, oxidative stress, and cell death signaling. Disruptions in mitochondrial calcium (
Language	English
Publishing date	2024-04-15
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	60-7
ISSN	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbadis.2024.167169
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Article: Post-translational modifications and protein quality control of mitochondrial channels and transporters.

Kadam, Ashlesha / Jadiya, Pooja / Tomar, Dhanendra

Frontiers in cell and developmental biology

2023 Volume 11, Page(s) 1196466

Abstract: Mitochondria play a critical role in energy metabolism and signal transduction, which is tightly regulated by proteins, metabolites, and ion fluxes. Metabolites and ion homeostasis are mainly mediated by channels and transporters present on mitochondrial ...

Abstract	Mitochondria play a critical role in energy metabolism and signal transduction, which is tightly regulated by proteins, metabolites, and ion fluxes. Metabolites and ion homeostasis are mainly mediated by channels and transporters present on mitochondrial membranes. Mitochondria comprise two distinct compartments, the outer mitochondrial membrane (OMM) and the inner mitochondrial membrane (IMM), which have differing permeabilities to ions and metabolites. The OMM is semipermeable due to the presence of non-selective molecular pores, while the IMM is highly selective and impermeable due to the presence of specialized channels and transporters which regulate ion and metabolite fluxes. These channels and transporters are modulated by various post-translational modifications (PTMs), including phosphorylation, oxidative modifications, ions, and metabolites binding, glycosylation, acetylation, and others. Additionally, the mitochondrial protein quality control (MPQC) system plays a crucial role in ensuring efficient molecular flux through the mitochondrial membranes by selectively removing mistargeted or defective proteins. Inefficient functioning of the transporters and channels in mitochondria can disrupt cellular homeostasis, leading to the onset of various pathological conditions. In this review, we provide a comprehensive overview of the current understanding of mitochondrial channels and transporters in terms of their functions, PTMs, and quality control mechanisms.
Language	English
Publishing date	2023-08-03
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2023.1196466
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Article ; Online: Mitochondrial Protein Quality Control Mechanisms.

Jadiya, Pooja / Tomar, Dhanendra

Genes

2020 Volume 11, Issue 5

Abstract: Mitochondria serve as a hub for many cellular processes, including bioenergetics, metabolism, cellular signaling, redox balance, calcium homeostasis, and cell death. The mitochondrial proteome includes over a thousand proteins, encoded by both the ... ...

Abstract	Mitochondria serve as a hub for many cellular processes, including bioenergetics, metabolism, cellular signaling, redox balance, calcium homeostasis, and cell death. The mitochondrial proteome includes over a thousand proteins, encoded by both the mitochondrial and nuclear genomes. The majority (~99%) of proteins are nuclear encoded that are synthesized in the cytosol and subsequently imported into the mitochondria. Within the mitochondria, polypeptides fold and assemble into their native functional form. Mitochondria health and integrity depend on correct protein import, folding, and regulated turnover termed as mitochondrial protein quality control (MPQC). Failure to maintain these processes can cause mitochondrial dysfunction that leads to various pathophysiological outcomes and the commencement of diseases. Here, we summarize the current knowledge about the role of different MPQC regulatory systems such as mitochondrial chaperones, proteases, the ubiquitin-proteasome system, mitochondrial unfolded protein response, mitophagy, and mitochondria-derived vesicles in the maintenance of mitochondrial proteome and health. The proper understanding of mitochondrial protein quality control mechanisms will provide relevant insights to treat multiple human diseases.
MeSH term(s)	Cell Nucleus/genetics ; Humans ; Mitochondria/genetics ; Mitochondrial Proteins/genetics ; Mitophagy/genetics ; Proteasome Endopeptidase Complex/genetics ; Protein Biosynthesis/genetics ; Protein Folding ; Ubiquitin/genetics ; Unfolded Protein Response/genetics
Chemical Substances	Mitochondrial Proteins ; Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2020-05-18
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2527218-4
ISSN	2073-4425 ; 2073-4425
ISSN (online)	2073-4425
ISSN	2073-4425
DOI	10.3390/genes11050563
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Article: Mitochondrial Protein Quality Control Mechanisms

Jadiya, Pooja / Tomar, Dhanendra

Genes. 2020 May 18, v. 11, no. 5

2020

Abstract	Mitochondria serve as a hub for many cellular processes, including bioenergetics, metabolism, cellular signaling, redox balance, calcium homeostasis, and cell death. The mitochondrial proteome includes over a thousand proteins, encoded by both the mitochondrial and nuclear genomes. The majority (~99%) of proteins are nuclear encoded that are synthesized in the cytosol and subsequently imported into the mitochondria. Within the mitochondria, polypeptides fold and assemble into their native functional form. Mitochondria health and integrity depend on correct protein import, folding, and regulated turnover termed as mitochondrial protein quality control (MPQC). Failure to maintain these processes can cause mitochondrial dysfunction that leads to various pathophysiological outcomes and the commencement of diseases. Here, we summarize the current knowledge about the role of different MPQC regulatory systems such as mitochondrial chaperones, proteases, the ubiquitin-proteasome system, mitochondrial unfolded protein response, mitophagy, and mitochondria-derived vesicles in the maintenance of mitochondrial proteome and health. The proper understanding of mitochondrial protein quality control mechanisms will provide relevant insights to treat multiple human diseases.
Keywords	calcium ; cell communication ; cytosol ; energy metabolism ; homeostasis ; human diseases ; mitochondria ; mitochondrial genome ; mitophagy ; polypeptides ; protein transport ; protein value ; proteinases ; proteins ; proteome ; quality control ; unfolded protein response
Language	English
Dates of publication	2020-0518
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2527218-4
ISSN	2073-4425
ISSN	2073-4425
DOI	10.3390/genes11050563
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Article ; Online: Neuronal loss of NCLX-dependent mitochondrial calcium efflux mediates age-associated cognitive decline.

Jadiya, Pooja / Cohen, Henry M / Kolmetzky, Devin W / Kadam, Ashlesha A / Tomar, Dhanendra / Elrod, John W

iScience

2023 Volume 26, Issue 3, Page(s) 106296

Abstract: Mitochondrial calcium overload contributes to neurodegenerative disease development and progression. We recently reported that loss of the mitochondrial sodium/calcium exchanger (NCLX), the primary mechanism ... ...

Abstract	Mitochondrial calcium overload contributes to neurodegenerative disease development and progression. We recently reported that loss of the mitochondrial sodium/calcium exchanger (NCLX), the primary mechanism of
Language	English
Publishing date	2023-02-28
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.106296
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Article ; Online: Reappraisal of metabolic dysfunction in neurodegeneration: Focus on mitochondrial function and calcium signaling.

Jadiya, Pooja / Garbincius, Joanne F / Elrod, John W

Acta neuropathologica communications

2021 Volume 9, Issue 1, Page(s) 124

Abstract: The cellular and molecular mechanisms that drive neurodegeneration remain poorly defined. Recent clinical trial failures, difficult diagnosis, uncertain etiology, and lack of curative therapies prompted us to re-examine other hypotheses of ... ...

Abstract	The cellular and molecular mechanisms that drive neurodegeneration remain poorly defined. Recent clinical trial failures, difficult diagnosis, uncertain etiology, and lack of curative therapies prompted us to re-examine other hypotheses of neurodegenerative pathogenesis. Recent reports establish that mitochondrial and calcium dysregulation occur early in many neurodegenerative diseases (NDDs), including Alzheimer's disease, Parkinson's disease, Huntington's disease, and others. However, causal molecular evidence of mitochondrial and metabolic contributions to pathogenesis remains insufficient. Here we summarize the data supporting the hypothesis that mitochondrial and metabolic dysfunction result from diverse etiologies of neuropathology. We provide a current and comprehensive review of the literature and interpret that defective mitochondrial metabolism is upstream and primary to protein aggregation and other dogmatic hypotheses of NDDs. Finally, we identify gaps in knowledge and propose therapeutic modulation of
MeSH term(s)	Animals ; Calcium Signaling/physiology ; Humans ; Mitochondria/metabolism ; Mitochondria/pathology ; Nerve Degeneration/metabolism ; Nerve Degeneration/pathology ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology
Language	English
Publishing date	2021-07-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-021-01224-4
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Article: MCU gain- and loss-of-function models define the duality of mitochondrial calcium uptake in heart failure.

Garbincius, Joanne F / Luongo, Timothy S / Lambert, Jonathan P / Mangold, Adam S / Murray, Emma K / Hildebrand, Alycia N / Jadiya, Pooja / Elrod, John W

bioRxiv : the preprint server for biology

2023

Abstract: Background: Mitochondrial calcium (: Objective: We tested the hypothesis that mtCU-dependent : Methods: Mice with tamoxifen-inducible, cardiomyocyte-specific gain (αMHC-MCM × flox-stop-MCU; MCU-Tg) or loss (αMHC-MCM × : Results: Cardiac ... ...

Abstract	Background: Mitochondrial calcium ( Objective: We tested the hypothesis that mtCU-dependent Methods: Mice with tamoxifen-inducible, cardiomyocyte-specific gain (αMHC-MCM × flox-stop-MCU; MCU-Tg) or loss (αMHC-MCM × Results: Cardiac contractility increased after 2d of isoproterenol in control, but not Conclusions: mtCU
Language	English
Publishing date	2023-04-18
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.04.17.537222
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Article ; Online: Osmotic stress induced toxicity exacerbates Parkinson's associated effects via dysregulation of autophagy in transgenic C. elegans model.

Jadiya, Pooja / Mir, Snober S / Nazir, Aamir

Cellular signalling

2018 Volume 45, Page(s) 71–80

Abstract: The accumulation of aggregate-prone proteins is a major representative of many neurological disorders, including Parkinson's disease (PD) wherein the cellular clearance mechanisms, such as the ubiquitin-proteasome and autophagy pathways are impaired. PD, ...

Abstract	The accumulation of aggregate-prone proteins is a major representative of many neurological disorders, including Parkinson's disease (PD) wherein the cellular clearance mechanisms, such as the ubiquitin-proteasome and autophagy pathways are impaired. PD, known to be associated with multiple genetic and environmental factors, is characterized by the aggregation of α-synuclein protein and loss of dopaminergic neurons in midbrain. This disease is also associated with other cardiovascular ailments. Herein, we report our findings from studies on the effect of hyper and hypo-osmotic induced toxicity representing hyper and hypotensive condition as an extrinsic epigenetic factor towards modulation of Parkinsonism, using a genetic model Caenorhabditis elegans (C. elegans). Our studies showed that osmotic toxicity had an adverse effect on α-synuclein aggregation, autophagic puncta, lipid content and oxidative stress. Further, we figure that reduced autophagic activity may cause the inefficient clearance of α-synuclein aggregates in osmotic stress toxicity, thereby promoting α-synuclein deposition. Pharmacological induction of autophagy by spermidine proved to be a useful mechanism for protecting cells against the toxic effects of these proteins in such stress conditions. Our studies provide evidence that autophagy is required for the removal of aggregated proteins in these conditions. Studying specific autophagy pathways, we observe that the osmotic stress induced toxicity was largely associated with atg-7 and lgg-1 dependent autophagy pathway, brought together by involvement of mTOR pathway. This represents a unifying pathway to disease in hyper- and hypo-osmotic conditions within PD model of C. elegans.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Autophagy ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/metabolism ; Disease Models, Animal ; Dopaminergic Neurons/metabolism ; Humans ; Lipid Metabolism ; Microtubule-Associated Proteins/metabolism ; Osmotic Pressure ; Oxidative Stress ; Parkinson Disease/pathology ; Spermidine/pharmacology ; Ubiquitin/metabolism ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; LGG-1 protein, C elegans ; Microtubule-Associated Proteins ; Ubiquitin ; alpha-Synuclein ; Spermidine (U87FK77H25)
Language	English
Publishing date	2018-02-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1002702-6
ISSN	1873-3913 ; 0898-6568
ISSN (online)	1873-3913
ISSN	0898-6568
DOI	10.1016/j.cellsig.2018.01.027
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Article: Human neurotropic polyomavirus, JC virus, agnoprotein targets mitochondrion and modulates its functions

Saxena, Reshu / Saribas, Sami / Jadiya, Pooja / Tomar, Dhanendra / Kaminski, Rafal / Elrod, John W / Safak, Mahmut

Virology. 2021 Jan. 15, v. 553

2021

Abstract: JC virus encodes an important regulatory protein, known as Agnoprotein (Agno). We have recently reported Agno's first protein-interactome with its cellular partners revealing that it targets various cellular networks and organelles, including ... ...

Abstract	JC virus encodes an important regulatory protein, known as Agnoprotein (Agno). We have recently reported Agno's first protein-interactome with its cellular partners revealing that it targets various cellular networks and organelles, including mitochondria. Here, we report further characterization of the functional consequences of its mitochondrial targeting and demonstrated its co-localization with the mitochondrial networks and with the mitochondrial outer membrane. The mitochondrial targeting sequence (MTS) of Agno and its dimerization domain together play major roles in this targeting. Data also showed alterations in various mitochondrial functions in Agno-positive cells; including a significant reduction in mitochondrial membrane potential, respiration rates and ATP production. In contrast, a substantial increase in ROS production and Ca²⁺ uptake by the mitochondria were also observed. Finally, findings also revealed a significant decrease in viral replication when Agno MTS was deleted, highlighting a role for MTS in the function of Agno during the viral life cycle.
Keywords	Human polyomavirus 2 ; calcium ; cell respiration ; cells ; dimerization ; humans ; membrane potential ; mitochondria ; mitochondrial membrane ; regulatory proteins ; virus replication
Language	English
Dates of publication	2021-0115
Size	p. 135-153.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-light
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2020.11.004
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Article ; Online: A pre- and co-knockdown of RNAseT enzyme, Eri-1, enhances the efficiency of RNAi induced gene silencing in Caenorhabditis elegans.

Jadiya, Pooja / Nazir, Aamir

PloS one

2014 Volume 9, Issue 1, Page(s) e87635

Abstract: Background: The approach of RNAi mediated gene knockdown, employing exogenous dsRNA, is being beneficially exploited in various fields of functional genomics. The immense utility of the approach came to fore from studies with model system C. elegans, ... ...

Abstract	Background: The approach of RNAi mediated gene knockdown, employing exogenous dsRNA, is being beneficially exploited in various fields of functional genomics. The immense utility of the approach came to fore from studies with model system C. elegans, but quickly became applicable with varied research models ranging from in vitro to various in vivo systems. Previously, there have been reports on the refractoriness of the neuronal cells to RNAi mediated gene silencing following which several modulators like eri-1 and lin-15 were described in C. elegans which, when present, would negatively impact the gene knockdown. Methodology/principal findings: Taking a clue from these findings, we went on to screen hypothesis-driven- methodologies towards exploring the efficiency in the process of RNAi under various experimental conditions, wherein these genes would be knocked down preceding to, or concurrently with, the knocking down of a gene of interest. For determining the efficiency of gene knockdown, we chose to study visually stark phenotypes of uncoordinated movement, dumpy body morphology and blistered cuticle obtained by knocking down of genes unc-73, dpy-9 and bli-3 respectively, employing the RNAi-by-feeding protocol in model system C. elegans. Conclusions/significance: Our studies led to a very interesting outcome as the results reveal that amongst various methods tested, pre-incubation with eri-1 dsRNA synthesizing bacteria followed by co-incubation with eri-1 and gene-of-interest dsRNA synthesizing bacteria leads to the most efficient gene silencing as observed by the analysis of marker phenotypes. This provides an approach for effectively employing RNAi induced gene silencing while working with different genetic backgrounds including transgenic and mutant strains.
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/antagonists & inhibitors ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Collagen/antagonists & inhibitors ; Collagen/genetics ; Collagen/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Exoribonucleases/antagonists & inhibitors ; Exoribonucleases/genetics ; Exoribonucleases/metabolism ; Gene Knockdown Techniques/methods ; Nerve Tissue Proteins/antagonists & inhibitors ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Oxidoreductases/antagonists & inhibitors ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Phenotype ; RNA Interference ; RNA, Double-Stranded/genetics ; RNA, Double-Stranded/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; Nerve Tissue Proteins ; RNA, Double-Stranded ; Repressor Proteins ; UNC-73 protein, C elegans ; lin-35 protein, C elegans ; Collagen (9007-34-5) ; Bli-3 protein, C elegans (EC 1.-) ; Oxidoreductases (EC 1.-) ; ERI-1 protein, C elegans (EC 3.1.-) ; Exoribonucleases (EC 3.1.-)
Language	English
Publishing date	2014-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0087635
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