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Article ; Online: ISG15 and ISGylation in Human Diseases.

Mirzalieva, Oygul / Juncker, Meredith / Schwartzenburg, Joshua / Desai, Shyamal

2022 Volume 11, Issue 3

Abstract: Type I Interferons (IFNs) induce the expression of >500 genes, which are collectively called ISGs (IFN-stimulated genes). One of the earliest ISGs induced by IFNs ... ...

Abstract	Type I Interferons (IFNs) induce the expression of >500 genes, which are collectively called ISGs (IFN-stimulated genes). One of the earliest ISGs induced by IFNs is
MeSH term(s)	Brain Injuries, Traumatic ; Cytokines/metabolism ; Humans ; Interferons/metabolism ; Neoplasms/genetics ; Ubiquitination ; Ubiquitins/genetics ; Ubiquitins/metabolism
Chemical Substances	Cytokines ; Ubiquitins ; ISG15 protein, human (60267-61-0) ; Interferons (9008-11-1)
Language	English
Publishing date	2022-02-04
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11030538
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Article ; Online: ISG15 and ISGylation in Human Diseases

Oygul Mirzalieva / Meredith Juncker / Joshua Schwartzenburg / Shyamal Desai

Cells, Vol 11, Iss 538, p

2022 Volume 538

Abstract: Type I Interferons (IFNs) induce the expression of >500 genes, which are collectively called ISGs (IFN-stimulated genes). One of the earliest ISGs induced by IFNs is ISG15 (Interferon-Stimulated Gene 15). Free ISG15 protein synthesized from the ISG15 ... ...

Abstract	Type I Interferons (IFNs) induce the expression of >500 genes, which are collectively called ISGs (IFN-stimulated genes). One of the earliest ISGs induced by IFNs is ISG15 (Interferon-Stimulated Gene 15). Free ISG15 protein synthesized from the ISG15 gene is post-translationally conjugated to cellular proteins and is also secreted by cells into the extracellular milieu. ISG15 comprises two ubiquitin-like domains (UBL1 and UBL2), each of which bears a striking similarity to ubiquitin, accounting for its earlier name ubiquitin cross-reactive protein (UCRP). Like ubiquitin, ISG15 harbors a characteristic β-grasp fold in both UBL domains. UBL2 domain has a conserved C-terminal Gly-Gly motif through which cellular proteins are appended via an enzymatic cascade similar to ubiquitylation called ISGylation. ISG15 protein is minimally expressed under physiological conditions. However, its IFN-dependent expression is aberrantly elevated or compromised in various human diseases, including multiple types of cancer, neurodegenerative disorders (Ataxia Telangiectasia and Amyotrophic Lateral Sclerosis), inflammatory diseases (Mendelian Susceptibility to Mycobacterial Disease (MSMD), bacteriopathy and viropathy), and in the lumbar spinal cords of veterans exposed to Traumatic Brain Injury (TBI). ISG15 and ISGylation have both inhibitory and/or stimulatory roles in the etiology and pathogenesis of human diseases. Thus, ISG15 is considered a “double-edged sword” for human diseases in which its expression is elevated. Because of the roles of ISG15 and ISGylation in cancer cell proliferation, migration, and metastasis, conferring anti-cancer drug sensitivity to tumor cells, and its elevated expression in cancer, neurodegenerative disorders, and veterans exposed to TBI, both ISG15 and ISGylation are now considered diagnostic/prognostic biomarkers and therapeutic targets for these ailments. In the current review, we shall cover the exciting journey of ISG15, spanning three decades from the bench to the bedside.
Keywords	ubiquitin ; ISG15 ; ISGylation ; cancer ; neurodegenerative diseases ; ISG15-deficient inflammatory diseases ; Biology (General) ; QH301-705.5
Subject code	610
Language	English
Publishing date	2022-02-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Increased ISGylation in Cases of TBI-Exposed ALS Veterans.

Schwartzenburg, Joshua / Juncker, Meredith / Reed, Ryan / Desai, Shyamal

Journal of neuropathology and experimental neurology

2019 Volume 78, Issue 3, Page(s) 209–218

Abstract: Veterans who have served in the military are at a nearly 60% greater risk of being diagnosed with amyotrophic lateral sclerosis (ALS). Literature reports suggest that a history of traumatic brain injury (TBI) may be a risk factor for ALS in veterans. ... ...

Abstract	Veterans who have served in the military are at a nearly 60% greater risk of being diagnosed with amyotrophic lateral sclerosis (ALS). Literature reports suggest that a history of traumatic brain injury (TBI) may be a risk factor for ALS in veterans. However, no diagnostic biomarkers are available for identifying ALS risk/development in TBI-exposed veterans. Here, using a Wes assay, we show that ISGylation, a conjugated form of interferon-stimulated gene 15 protein, is significantly elevated in the lumbar spinal cords (SC-Ls) of TBI-ALS compared with ALS veterans without a previous history of TBI (nonTBI-ALS). Although not as striking as in TBI-ALS veterans, ISGylation is also increased in nonTBI-ALS compared with normal veterans. Notably, no changes in ISGylation were seen in occipital lobe samples obtained from the same patients, suggesting that elevated ISGylation is distinct to ALS disease-specific SC-Ls. Moreover, we detected increased ISGylation in cerebral spinal fluid samples of TBI-ALS veterans. Other results using cultured lymphocyte cell lines show a similar trend of increased ISGylation in ALS patients from the general population. Together, these data suggest that ISGylation could serve as a diagnostic biomarker for TBI-ALS veterans, nonTBI-ALS veterans, and nonveterans affected by ALS.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Amyotrophic Lateral Sclerosis/diagnosis ; Amyotrophic Lateral Sclerosis/epidemiology ; Amyotrophic Lateral Sclerosis/metabolism ; Brain Injuries, Traumatic/diagnosis ; Brain Injuries, Traumatic/epidemiology ; Brain Injuries, Traumatic/metabolism ; Cytokines/metabolism ; Female ; Humans ; Male ; Middle Aged ; Ubiquitins/metabolism ; Veterans
Chemical Substances	Cytokines ; Ubiquitins ; ISG15 protein, human (60267-61-0)
Language	English
Publishing date	2019-01-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3088-0
ISSN	1554-6578 ; 0022-3069
ISSN (online)	1554-6578
ISSN	0022-3069
DOI	10.1093/jnen/nly129
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Article ; Online: ISGylation is increased in the peripheral blood mononuclear cells derived from symptomatic COVID-19 patients.

Schwartzenburg, Joshua / Reed, Ryan / Koul, Hari / Zea, Arnold H / Shellito, Judd / Miele, Lucio / Crabtree, Judy S / Desai, Shyamal

Experimental biology and medicine (Maywood, N.J.)

2022 Volume 247, Issue 10, Page(s) 842–847

Abstract: Cytokine-driven hyper inflammation has been identified as a critical factor behind poor outcomes in patients severely infected with SARS-CoV-2 virus. Notably, protein ISGylation, a protein conjugated form of Type 1 IFN-inducible ubiquitin-like protein ... ...

Abstract	Cytokine-driven hyper inflammation has been identified as a critical factor behind poor outcomes in patients severely infected with SARS-CoV-2 virus. Notably, protein ISGylation, a protein conjugated form of Type 1 IFN-inducible ubiquitin-like protein ISG15 (
MeSH term(s)	Animals ; COVID-19 ; Cytokines/metabolism ; Humans ; Inflammation ; Leukocytes, Mononuclear/metabolism ; Mice ; SARS-CoV-2 ; Ubiquitins/metabolism
Chemical Substances	Cytokines ; Ubiquitins
Language	English
Publishing date	2022-02-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	4015-0
ISSN	1535-3699 ; 1525-1373 ; 0037-9727
ISSN (online)	1535-3699 ; 1525-1373
ISSN	0037-9727
DOI	10.1177/15353702221075606
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Article ; Online: ISG15 attenuates post-translational modifications of mitofusins and congression of damaged mitochondria in Ataxia Telangiectasia cells.

Juncker, Meredith / Kim, Catherine / Reed, Ryan / Haas, Arthur / Schwartzenburg, Joshua / Desai, Shyamal

Biochimica et biophysica acta. Molecular basis of disease

2021 Volume 1867, Issue 6, Page(s) 166102

Abstract: Mitophagy is defective in several neurodegenerative diseases, including Ataxia Telangiectasia (A-T). However, the molecular mechanism underlying defective mitophagy in A-T is unknown. Literature indicates that damaged mitochondria are transported to the ... ...

Abstract	Mitophagy is defective in several neurodegenerative diseases, including Ataxia Telangiectasia (A-T). However, the molecular mechanism underlying defective mitophagy in A-T is unknown. Literature indicates that damaged mitochondria are transported to the perinuclear region prior to their removal via mitophagy. Our previous work has indicated that conjugation of SUMO2 (Small Ubiquitin-like Modifier 2) to mitofusins (Mfns) may be necessary for congression of mitochondria into SUMO2-/ubiquitin-/LC3-positive compact structures resembling mito-aggresomes at the perinuclear region in CCCP-treated HEK293 cells. Here, we demonstrate that Mfns are SUMOylated, and mitochondria are transported to the perinuclear region; however, mitochondria fail to congress into mito-aggresome-like structures in CCCP-treated A-T cells. Defect in mitochondrial congression is causally related to constitutively elevated ISG15 (Interferon-Stimulated Gene 15), an antagonist of the ubiquitin pathway, in A-T cells. Suppression of the ISG15 pathway restores mitochondrial congression, reduce oxidative stress, and level of unhealthy mitochondria, which is suggestive of restoration of mitophagy in A-T cells. ISG15 is also constitutively elevated and mitophagy is defective in Amytrophic Lateral Sclerosis (ALS). The constitutively elevated ISG15 pathway therefore appears to be a common unifying biochemical mechanism underlying defective mitophagy in neurodegenerative disorders thus, implying the broader significance of our findings, and suggest the potential role of ISG15 inhibitors in their treatment.
MeSH term(s)	Ataxia Telangiectasia/genetics ; Ataxia Telangiectasia/metabolism ; Ataxia Telangiectasia/pathology ; Cytokines/genetics ; Cytokines/metabolism ; GTP Phosphohydrolases/chemistry ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; HEK293 Cells ; Humans ; Mitochondria/metabolism ; Mitochondria/pathology ; Mitochondrial Membrane Transport Proteins/chemistry ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitophagy ; Protein Processing, Post-Translational ; Ubiquitin/metabolism ; Ubiquitins/genetics ; Ubiquitins/metabolism
Chemical Substances	Cytokines ; Mitochondrial Membrane Transport Proteins ; Ubiquitin ; Ubiquitins ; ISG15 protein, human (60267-61-0) ; GTP Phosphohydrolases (EC 3.6.1.-) ; Mfn1 protein, human (EC 3.6.5.-)
Language	English
Publishing date	2021-02-19
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
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.2021.166102
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Article ; Online: Neuropathological Outcomes of Traumatic Brain Injury and Alcohol Use in Males and Females: Studies Using Pre-Clinical Rodent and Clinical Human Specimens.

Schwartzenburg, Joshua B / Cruise, Shealan C / Reed, Ryan E / Hutchinson, Corrine M / Mirzalieva, Oygul S / Edwards, Kimberly N / Edwards, Scott / Gilpin, Nicholas W / Molina, Patricia E / Desai, Shyamal D

Journal of neurotrauma

2023 Volume 40, Issue 21-22, Page(s) 2410–2426

Abstract: Traumatic brain injury (TBI) and alcohol misuse are inextricably linked and can increase the risk for development of neurodegenerative diseases, particularly in military veterans and contact sport athletes. Proteinopathy (defects in protein degradation) ... ...

Abstract	Traumatic brain injury (TBI) and alcohol misuse are inextricably linked and can increase the risk for development of neurodegenerative diseases, particularly in military veterans and contact sport athletes. Proteinopathy (defects in protein degradation) is considered an underlying factor in neurodegenerative diseases. Whether it contributes to TBI/alcohol-mediated neurodegeneration is unexplored, however. Our recent studies have identified ISGylation, a conjugated form of ISG15 (Interferon-Stimulated Gene 15) and inducer of proteinopathy, as a potential mechanistic link underlying TBI-mediated neurodegeneration and proteinopathy in veterans. In the current study, a rat model of combined TBI and alcohol use was utilized to investigate the same relationship. Here, we report sustained induction of Interferon β (IFNβ), changes in TAR DNA Binding 43 (TDP-43) ISGylation levels, TDP-43 proteinopathy (C-terminal fragmentation [CTF]), and neurodegeneration in the ventral horns of the lumbar spinal cords (LSCs) and/or motor cortices (MCs) of female rats post-TBI in a time-dependent manner. In males, these findings mostly remained non-significant, although moderate alcohol use appears to decrease neurodegeneration in males (but not females) post-TBI. We, however, do not claim that moderate alcohol consumption is beneficial for preventing TBI-mediated neurodegeneration. We have previously demonstrated that ISGylation is increased in the LSCs of veterans with TBI/ALS (amyotrophic lateral sclerosis). Here, we show increased ISGylation of TDP-43 in the LSCs of TBI/ALS-afflicted female veterans compared with male veterans. Knowing that ISGylation induces proteinopathy, we suggest targeting ISGylation may prevent proteinopathy-mediated neurodegeneration post-TBI, particularly in women; however, causal studies are required to confirm this claim.
MeSH term(s)	Humans ; Male ; Female ; Animals ; Rats ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Rodentia/metabolism ; Brain Injuries, Traumatic/metabolism ; DNA-Binding Proteins/genetics ; Chronic Traumatic Encephalopathy ; Alcohol Drinking
Chemical Substances	DNA-Binding Proteins
Language	English
Publishing date	2023-07-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	645092-1
ISSN	1557-9042 ; 0897-7151
ISSN (online)	1557-9042
ISSN	0897-7151
DOI	10.1089/neu.2023.0074
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Article ; Online: SUMOylation of mitofusins: A potential mechanism for perinuclear mitochondrial congression in cells treated with mitochondrial stressors.

Kim, Catherine / Juncker, Meredith / Reed, Ryan / Haas, Arthur / Guidry, Jessie / Matunis, Michael / Yang, Wei-Chih / Schwartzenburg, Joshua / Desai, Shyamal

Biochimica et biophysica acta. Molecular basis of disease

2021 Volume 1867, Issue 6, Page(s) 166104

Abstract: Depolarized/damaged mitochondria aggregate at the perinuclear region prior to mitophagy in cells treated with mitochondrial stressors. However, the cellular mechanism(s) by which damaged mitochondria are transported and remain aggregated at the ... ...

Abstract	Depolarized/damaged mitochondria aggregate at the perinuclear region prior to mitophagy in cells treated with mitochondrial stressors. However, the cellular mechanism(s) by which damaged mitochondria are transported and remain aggregated at the perinuclear region is unknown. Here, we demonstrate that mitofusins (Mfn1/2) are post-translationally modified by SUMO2 (Small Ubiquitin-related Modifier 2) in Human embryonic kidney 293 (Hek293) cells treated with protonophore CCCP and proteasome inhibitor MG132, both known mitochondrial stressors. SUMOylation of Mfn1/2 is not for their proteasomal degradation but facilitate mitochondrial congression at the perinuclear region in CCCP- and MG132-treated cells. Additionally, congressed mitochondria (mito-aggresomes) colocalize with LC3, ubiquitin, and SUMO2 in CCCP-treated cells. Knowing that SUMO functions as a "molecular glue" to facilitate protein-protein interactions, we propose that SUMOylation of Mfn1/2 may congress, glues, and confines damaged mitochondria to the perinuclear region thereby, protectively quarantining them from the heathy mitochondrial network until their removal via mitophagy in cells.
MeSH term(s)	Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Cell Nucleus/metabolism ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; HEK293 Cells ; Humans ; Mitochondria/drug effects ; Mitochondria/metabolism ; Mitochondria/pathology ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitophagy ; Proton Ionophores/pharmacology ; Stress, Physiological ; Sumoylation
Chemical Substances	Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Proton Ionophores ; Carbonyl Cyanide m-Chlorophenyl Hydrazone (555-60-2) ; GTP Phosphohydrolases (EC 3.6.1.-) ; MFN2 protein, human (EC 3.6.1.-) ; Mfn1 protein, human (EC 3.6.5.-)
Language	English
Publishing date	2021-02-19
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
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.2021.166104
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Article ; Online: Identification and characterization of a solute carrier, CIA8, involved in inorganic carbon acclimation in Chlamydomonas reinhardtii.

Machingura, Marylou C / Bajsa-Hirschel, Joanna / Laborde, Susan M / Schwartzenburg, Joshua B / Mukherjee, Bratati / Mukherjee, Ananya / Pollock, Steve V / Förster, Britta / Price, G Dean / Moroney, James V

Journal of experimental botany

2017 Volume 68, Issue 14, Page(s) 3879–3890

Abstract: The supply of inorganic carbon (Ci) at the site of fixation by Rubisco is a key parameter for efficient CO2 fixation in aquatic organisms including the green alga, Chlamydomonas reinhardtii. Chlamydomonas reinhardtii cells, when grown on limiting CO2, ... ...

Abstract	The supply of inorganic carbon (Ci) at the site of fixation by Rubisco is a key parameter for efficient CO2 fixation in aquatic organisms including the green alga, Chlamydomonas reinhardtii. Chlamydomonas reinhardtii cells, when grown on limiting CO2, have a CO2-concentrating mechanism (CCM) that functions to concentrate CO2 at the site of Rubisco. Proteins thought to be involved in inorganic carbon uptake have been identified and localized to the plasma membrane or chloroplast envelope. However, current CCM models suggest that additional molecular components are involved in Ci uptake. In this study, the gene Cia8 was identified in an insertional mutagenesis screen and characterized. The protein encoded by Cia8 belongs to the sodium bile acid symporter subfamily. Transcript levels for this gene were significantly up-regulated when the cells were grown on low CO2. The cia8 mutant exhibited reduced growth and reduced affinity for Ci when grown in limiting CO2 conditions. Prediction programs localize this protein to the chloroplast. Ci uptake and the photosynthetic rate, particularly at high external pH, were reduced in the mutant. The results are consistent with the model that CIA8 is involved in Ci uptake in C. reinhardtii.
MeSH term(s)	Algal Proteins/genetics ; Algal Proteins/metabolism ; Carbon/metabolism ; Carbon Compounds, Inorganic/metabolism ; Chlamydomonas reinhardtii/genetics ; Chlamydomonas reinhardtii/metabolism ; Chloroplast Proteins/genetics ; Chloroplast Proteins/metabolism ; Photosynthesis ; Up-Regulation
Chemical Substances	Algal Proteins ; Carbon Compounds, Inorganic ; Chloroplast Proteins ; Carbon (7440-44-0)
Language	English
Publishing date	2017--01
Publishing country	England
Document type	Journal Article
ZDB-ID	2976-2
ISSN	1460-2431 ; 0022-0957
ISSN (online)	1460-2431
ISSN	0022-0957
DOI	10.1093/jxb/erx189
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