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Article: Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes.

Nikonorova, Inna A / desRanleau, Elizabeth / Jacobs, Katherine C / Saul, Joshua / Walsh, Jonathon D / Wang, Juan / Barr, Maureen M

bioRxiv : the preprint server for biology

2024

Abstract: Therapeutic use of tiny extracellular vesicles (EVs) requires understanding cargo loading mechanisms. Here, we used a modular proximity label approach to identify EV cargo associated with the transient potential channel (TRP) polycystin PKD-2 ... ...

Abstract	Therapeutic use of tiny extracellular vesicles (EVs) requires understanding cargo loading mechanisms. Here, we used a modular proximity label approach to identify EV cargo associated with the transient potential channel (TRP) polycystin PKD-2 of
Language	English
Publishing date	2024-04-18
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.04.17.588758
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Article: Ciliary intrinsic mechanisms regulate dynamic ciliary extracellular vesicle release from sensory neurons.

Wang, Juan / Saul, Josh / Nikonorova, Inna A / Cruz, Carlos Nava / Power, Kaiden M / Nguyen, Ken C / Hall, David H / Barr, Maureen M

bioRxiv : the preprint server for biology

2023

Abstract: Cilia-derived extracellular vesicles (EVs) contain signaling proteins and act in intercellular communication. Polycystin-2 (PKD-2), a transient receptor potential channel, is a conserved ciliary EVs cargo. ...

Abstract	Cilia-derived extracellular vesicles (EVs) contain signaling proteins and act in intercellular communication. Polycystin-2 (PKD-2), a transient receptor potential channel, is a conserved ciliary EVs cargo.
Language	English
Publishing date	2023-11-03
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.11.01.565151
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Article ; Online: Tracking N- and C-termini of C. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles.

Walsh, Jonathon D / Wang, Juan / DeHart, Molly / Nikonorova, Inna A / Srinivasan, Jagan / Barr, Maureen M

PLoS genetics

2022 Volume 18, Issue 12, Page(s) e1010560

Abstract: The cilium acts as an antenna receiving and sending signals, the latter via extracellular vesicles (EVs). In C. elegans and mammals, the Autosomal Dominant Polycystic Kidney Disease (ADPKD) gene products polycystin-1 (PC1) and polycystin-2 (PC2) localize ...

Abstract	The cilium acts as an antenna receiving and sending signals, the latter via extracellular vesicles (EVs). In C. elegans and mammals, the Autosomal Dominant Polycystic Kidney Disease (ADPKD) gene products polycystin-1 (PC1) and polycystin-2 (PC2) localize to both cilia and EVs, act in the same genetic pathway, and function in a sensory capacity, suggesting ancient conservation. However, the functions of the polycystins on cilia and EVs remain enigmatic. We used our C. elegans model and endogenously fluorescent-tagged LOV-1/polycystin-1 to study LOV-1 processing, trafficking, transport, EV biogenesis, and function in living animals. Super resolution, real time imaging reveals that LOV-1 is processed into N-terminal (NTM) and C-terminal (CTM) forms via a conserved GPCR proteolytic site (GPS). The LOV-1 NTM is secreted into the extracellular matrix and not localized to ciliary tip EVs. In contrast, LOV-1 CTM and PKD-2 are co-trafficked, co-transported, and co-localized in cilia and on environmentally released ciliary EVs. LOV-1 CTM requires PKD-2 for ciliary EV localization, while PKD-2 localizes to ciliary EVs independent of LOV-1. We find that LOV-1 but not PKD-2 is required for chemosensation of an ascaroside mating pheromone. These findings indicate that the polycystins LOV-1 and PKD-2 function together and independently and provide insight to how cargo is selected and packaged in ciliary EVs.
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cilia/genetics ; Cilia/metabolism ; Extracellular Vesicles/genetics ; Extracellular Vesicles/metabolism ; TRPP Cation Channels/genetics
Chemical Substances	Caenorhabditis elegans Proteins ; TRPP Cation Channels ; LOV-1 protein, C elegans ; PKD-2 protein, C elegans
Language	English
Publishing date	2022-12-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1010560
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Article ; Online: Release and targeting of polycystin-2-carrying ciliary extracellular vesicles.

Wang, Juan / Nikonorova, Inna A / Gu, Amanda / Sternberg, Paul W / Barr, Maureen M

Current biology : CB

2020 Volume 30, Issue 13, Page(s) R755–R756

MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cilia/metabolism ; Extracellular Vesicles/metabolism ; Hermaphroditic Organisms/genetics ; Hermaphroditic Organisms/physiology ; Male ; Protein Transport ; Reproduction ; TRPP Cation Channels/genetics ; TRPP Cation Channels/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; PKD-2 protein, C elegans ; TRPP Cation Channels
Language	English
Publishing date	2020-08-04
Publishing country	England
Document type	Letter ; Research Support, N.I.H., Extramural
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2020.05.079
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Article ; Online: Sensory cilia act as a specialized venue for regulated extracellular vesicle biogenesis and signaling.

Wang, Juan / Nikonorova, Inna A / Silva, Malan / Walsh, Jonathon D / Tilton, Peter E / Gu, Amanda / Akella, Jyothi S / Barr, Maureen M

Current biology : CB

2021 Volume 31, Issue 17, Page(s) 3943–3951.e3

Abstract: Ciliary extracellular vesicle (EV) shedding is evolutionarily conserved. In Chlamydomonas and C. elegans, ciliary EVs act as signaling devices. ...

Abstract	Ciliary extracellular vesicle (EV) shedding is evolutionarily conserved. In Chlamydomonas and C. elegans, ciliary EVs act as signaling devices.
MeSH term(s)	Animals ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cilia/metabolism ; Extracellular Vesicles/metabolism ; Male ; Mammals ; Protein Transport
Chemical Substances	Caenorhabditis elegans Proteins
Language	English
Publishing date	2021-07-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2021.06.040
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Article ; Online: Isolation, profiling, and tracking of extracellular vesicle cargo in Caenorhabditis elegans.

Nikonorova, Inna A / Wang, Juan / Cope, Alexander L / Tilton, Peter E / Power, Kaiden M / Walsh, Jonathon D / Akella, Jyothi S / Krauchunas, Amber R / Shah, Premal / Barr, Maureen M

Current biology : CB

2022 Volume 32, Issue 9, Page(s) 1924–1936.e6

Abstract: Extracellular vesicles (EVs) may mediate intercellular communication by carrying protein and RNA cargo. The composition, biology, and roles of EVs in physiology and pathology have been primarily studied in the context of biofluids and in cultured ... ...

Abstract	Extracellular vesicles (EVs) may mediate intercellular communication by carrying protein and RNA cargo. The composition, biology, and roles of EVs in physiology and pathology have been primarily studied in the context of biofluids and in cultured mammalian cells. The experimental tractability of C. elegans makes for a powerful in vivo animal system to identify and study EV cargo from its cellular source. We developed an innovative method to label, track, and profile EVs using genetically encoded, fluorescent-tagged EV cargo and conducted a large-scale isolation and proteomic profiling. Nucleic acid binding proteins (∼200) are overrepresented in our dataset. By integrating our EV proteomic dataset with single-cell transcriptomic data, we identified and validated ciliary EV cargo: CD9-like tetraspanin (TSP-6), ectonucleotide pyrophosphatase/phosphodiesterase (ENPP-1), minichromosome maintenance protein (MCM-3), and double-stranded RNA transporter SID-2. C. elegans EVs also harbor RNA, suggesting that EVs may play a role in extracellular RNA-based communication.
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Cell Communication ; Extracellular Vesicles/metabolism ; Mammals/genetics ; Proteomics ; RNA
Chemical Substances	RNA (63231-63-0)
Language	English
Publishing date	2022-03-24
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2022.03.005
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Article ; Online: Time-resolved analysis of amino acid stress identifies eIF2 phosphorylation as necessary to inhibit mTORC1 activity in liver.

Nikonorova, Inna A / Mirek, Emily T / Signore, Christina C / Goudie, Michael P / Wek, Ronald C / Anthony, Tracy G

The Journal of biological chemistry

2018 Volume 293, Issue 14, Page(s) 5005–5015

Abstract: Amino acid availability is sensed by GCN2 (general control nonderepressible 2) and mechanistic target of rapamycin complex 1 (mTORC1), but how these two sensors coordinate their respective signal transduction events remains mysterious. In this study we ... ...

Abstract	Amino acid availability is sensed by GCN2 (general control nonderepressible 2) and mechanistic target of rapamycin complex 1 (mTORC1), but how these two sensors coordinate their respective signal transduction events remains mysterious. In this study we utilized mouse genetic models to investigate the role of GCN2 in hepatic mTORC1 regulation upon amino acid stress induced by a single injection of asparaginase. We found that deletion of
MeSH term(s)	Amino Acids/metabolism ; Animals ; Eukaryotic Initiation Factor-2/metabolism ; Female ; Gene Deletion ; Liver/metabolism ; Male ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Mice, Inbred C57BL ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction
Chemical Substances	Amino Acids ; Eukaryotic Initiation Factor-2 ; Eif2ak4 protein, mouse (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2018-02-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA117.001625
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Article ; Online: Identification of a Mg2+-sensitive ORF in the 5'-leader of TRPM7 magnesium channel mRNA.

Nikonorova, Inna A / Kornakov, Nikolay V / Dmitriev, Sergey E / Vassilenko, Konstantin S / Ryazanov, Alexey G

Nucleic acids research

2014 Volume 42, Issue 20, Page(s) 12779–12788

Abstract: TRPM7 is an essential and ubiquitous channel-kinase regulating cellular influx of Mg2+. Although TRPM7 mRNA is highly abundant, very small amount of the protein is detected in cells, suggesting post-transcriptional regulation of trpm7 gene expression. We ...

Abstract	TRPM7 is an essential and ubiquitous channel-kinase regulating cellular influx of Mg2+. Although TRPM7 mRNA is highly abundant, very small amount of the protein is detected in cells, suggesting post-transcriptional regulation of trpm7 gene expression. We found that TRPM7 mRNA 5'-leader contains two evolutionarily conserved upstream open reading frames that act together to drastically inhibit translation of the TRPM7 reading frame at high magnesium levels and ensure its optimal translation at low magnesium levels, when the activity of the channel-kinase is most required. The study provides the first example of magnesium channel synthesis being controlled by Mg2+ in higher eukaryotes.
MeSH term(s)	5' Untranslated Regions ; Base Sequence ; Conserved Sequence ; Gene Expression Regulation ; HEK293 Cells ; Humans ; Magnesium/pharmacology ; Open Reading Frames ; Protein Biosynthesis/drug effects ; TRPM Cation Channels/genetics
Chemical Substances	5' Untranslated Regions ; TRPM Cation Channels ; Trpm7 protein, mouse (EC 2.7.1.-) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2014-10-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gku951
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Article ; Online: Age modulates liver responses to asparaginase-induced amino acid stress in mice.

Nikonorova, Inna A / Zhu, Qiaoqiao / Signore, Christina C / Mirek, Emily T / Jonsson, William O / Kong, Bo / Guo, Grace L / Belden, William J / Anthony, Tracy G

The Journal of biological chemistry

2019 Volume 294, Issue 38, Page(s) 13864–13875

Abstract: Asparaginase is an amino acid-depleting agent used to treat blood cancers. Metabolic complications due to asparaginase affect liver function in humans. To examine how the liver response to asparaginase changes during maturity to adulthood, here we ... ...

Abstract	Asparaginase is an amino acid-depleting agent used to treat blood cancers. Metabolic complications due to asparaginase affect liver function in humans. To examine how the liver response to asparaginase changes during maturity to adulthood, here we treated juvenile (2-week), young adult (8-week), and mature adult (16-week) mice with drug or excipient for 1 week and conducted RNA-Seq and functional analyses. Asparaginase reduced body growth and liver mass in juveniles but not in the adult animals. Unbiased exploration of the effect of asparaginase on the liver transcriptome revealed that the
MeSH term(s)	Age Factors ; Amino Acids/metabolism ; Animals ; Asparaginase/adverse effects ; Asparaginase/metabolism ; Asparaginase/physiology ; Eukaryotic Initiation Factor-2/metabolism ; Fatty Liver/metabolism ; Female ; Liver/metabolism ; Liver/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Stress, Physiological/drug effects ; Transcriptome/drug effects ; Transcriptome/genetics
Chemical Substances	Amino Acids ; Eukaryotic Initiation Factor-2 ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Asparaginase (EC 3.5.1.1)
Language	English
Publishing date	2019-08-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.009864
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Article ; Online: Role of activating transcription factor 4 in the hepatic response to amino acid depletion by asparaginase.

Al-Baghdadi, Rana J T / Nikonorova, Inna A / Mirek, Emily T / Wang, Yongping / Park, Jinhee / Belden, William J / Wek, Ronald C / Anthony, Tracy G

Scientific reports

2017 Volume 7, Issue 1, Page(s) 1272

Abstract: The anti-leukemic agent asparaginase activates the integrated stress response (ISR) kinase GCN2 and inhibits signaling via mechanistic target of rapamycin complex 1 (mTORC1). The study objective was to investigate the protective role of activating ... ...

Abstract	The anti-leukemic agent asparaginase activates the integrated stress response (ISR) kinase GCN2 and inhibits signaling via mechanistic target of rapamycin complex 1 (mTORC1). The study objective was to investigate the protective role of activating transcription factor 4 (ATF4) in controlling the hepatic transcriptome and mediating GCN2-mTORC1 signaling during asparaginase. We compared global gene expression patterns in livers from wildtype, Gcn2 Conclusions: GCN2 and ATF4 serve complementary roles in the hepatic response to asparaginase. GCN2 functions to limit inflammation and mTORC1 signaling whereas ATF4 serves to limit the amino acid response and prevent ER stress during amino acid depletion by asparaginase.
MeSH term(s)	Activating Transcription Factor 4/genetics ; Activating Transcription Factor 4/metabolism ; Amino Acids/metabolism ; Animals ; Antineoplastic Agents/administration & dosage ; Antineoplastic Agents/metabolism ; Asparaginase/administration & dosage ; Asparaginase/metabolism ; Endoplasmic Reticulum Stress ; Gene Expression Profiling ; Liver/pathology ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Mice ; Mice, Knockout ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism
Chemical Substances	Amino Acids ; Antineoplastic Agents ; Atf4 protein, mouse ; Activating Transcription Factor 4 (145891-90-3) ; Eif2ak4 protein, mouse (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Asparaginase (EC 3.5.1.1)
Language	English
Publishing date	2017-04-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-01041-7
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