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  1. Article ; Online: Jeremy Jon Kaye, MD.

    Nance, E Paul / Miller, Theodore T

    Radiology

    2016  Volume 279, Issue 2, Page(s) 656

    MeSH term(s) History, 20th Century ; History, 21st Century ; Radiology/history ; United States
    Language English
    Publishing date 2016-05
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article ; Portraits
    ZDB-ID 80324-8
    ISSN 1527-1315 ; 0033-8419
    ISSN (online) 1527-1315
    ISSN 0033-8419
    DOI 10.1148/radiol.2016164010
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  2. Article ; Online: Germline TFAM levels regulate mitochondrial DNA copy number and mutant heteroplasmy in

    Schwartz, Aaron Z A / Nance, Jeremy

    microPublication biology

    2023  Volume 2023

    Abstract: The mitochondrial genome (mtDNA) is packaged into discrete protein-DNA complexes called nucleoids. mtDNA packaging factor TFAM (mitochondrial transcription factor-A) promotes nucleoid compaction and is required for mtDNA replication. Here, we investigate ...

    Abstract The mitochondrial genome (mtDNA) is packaged into discrete protein-DNA complexes called nucleoids. mtDNA packaging factor TFAM (mitochondrial transcription factor-A) promotes nucleoid compaction and is required for mtDNA replication. Here, we investigate how changing TFAM levels affects mtDNA in the
    Language English
    Publishing date 2023-02-14
    Publishing country United States
    Document type Journal Article
    ISSN 2578-9430
    ISSN (online) 2578-9430
    DOI 10.17912/micropub.biology.000727
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: C. elegans Afadin is required for epidermal morphogenesis and functionally interfaces with the cadherin-catenin complex and RhoGAP PAC-1/ARHGAP21.

    Hall, Allison E / Klompstra, Diana / Nance, Jeremy

    Developmental biology

    2024  Volume 511, Page(s) 12–25

    Abstract: During epithelial morphogenesis, the apical junctions connecting cells must remodel as cells change shape and make new connections with their neighbors. In the C. elegans embryo, new apical junctions form when epidermal cells migrate and seal with one ... ...

    Abstract During epithelial morphogenesis, the apical junctions connecting cells must remodel as cells change shape and make new connections with their neighbors. In the C. elegans embryo, new apical junctions form when epidermal cells migrate and seal with one another to encase the embryo in skin ('ventral enclosure'), and junctions remodel when epidermal cells change shape to squeeze the embryo into a worm shape ('elongation'). The junctional cadherin-catenin complex (CCC), which links epithelial cells to each other and to cortical actomyosin, is essential for C. elegans epidermal morphogenesis. RNAi genetic enhancement screens have identified several genes encoding proteins that interact with the CCC to promote epidermal morphogenesis, including the scaffolding protein Afadin (AFD-1), whose depletion alone results in only minor morphogenesis defects. Here, by creating a null mutation in afd-1, we show that afd-1 provides a significant contribution to ventral enclosure and elongation on its own. Unexpectedly, we find that afd-1 mutant phenotypes are strongly modified by diet, revealing a previously unappreciated parental nutritional input to morphogenesis. We identify functional interactions between AFD-1 and the CCC by demonstrating that E-cadherin is required for the polarized distribution of AFD-1 to cell contact sites in early embryos. Finally, we show that afd-1 promotes the enrichment of polarity regulator, and CCC-interacting protein, PAC-1/ARHGAP21 to cell contact sites, and we identify genetic interactions suggesting that afd-1 and pac-1 regulate epidermal morphogenesis at least in part through parallel mechanisms. Our findings reveal that C. elegans AFD-1 makes a significant contribution to epidermal morphogenesis and functionally interfaces with core and associated CCC proteins.
    Language English
    Publishing date 2024-03-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1114-9
    ISSN 1095-564X ; 0012-1606
    ISSN (online) 1095-564X
    ISSN 0012-1606
    DOI 10.1016/j.ydbio.2024.03.007
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  4. Article: C. elegans

    Hall, Allison E / Klompstra, Diana / Nance, Jeremy

    bioRxiv : the preprint server for biology

    2023  

    Abstract: During epithelial morphogenesis, the apical junctions connecting cells must remodel as cells change shape and make new connections with their neighbors. In ... ...

    Abstract During epithelial morphogenesis, the apical junctions connecting cells must remodel as cells change shape and make new connections with their neighbors. In the
    Language English
    Publishing date 2023-07-30
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.07.28.551013
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  5. Article: ZIF-1-mediated degradation of endogenous and heterologous zinc finger proteins in the

    Schwartz, Aaron Z A / Abdu, Yusuff / Nance, Jeremy

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Rapid and conditional protein depletion is the gold standard genetic tool for deciphering the molecular basis of developmental processes. Previously, we showed that by conditionally expressing the E3 ligase substrate adaptor ZIF-1 ... ...

    Abstract Rapid and conditional protein depletion is the gold standard genetic tool for deciphering the molecular basis of developmental processes. Previously, we showed that by conditionally expressing the E3 ligase substrate adaptor ZIF-1 in
    Language English
    Publishing date 2023-07-10
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.07.10.548405
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: ZIF-1-mediated degradation of zinc finger proteins in the Caenorhabditis elegans germ line.

    Schwartz, Aaron Z A / Abdu, Yusuff / Nance, Jeremy

    Genetics

    2023  Volume 225, Issue 3

    Abstract: Rapid and conditional protein depletion is the gold standard genetic tool for deciphering the molecular basis of developmental processes. Previously, we showed that by conditionally expressing the E3 ligase substrate adaptor ZIF-1 in Caenorhabditis ... ...

    Abstract Rapid and conditional protein depletion is the gold standard genetic tool for deciphering the molecular basis of developmental processes. Previously, we showed that by conditionally expressing the E3 ligase substrate adaptor ZIF-1 in Caenorhabditis elegans somatic cells, proteins tagged with the first CCCH Zn finger 1 (ZF1) domain from the germline regulator PIE-1 degrade rapidly, resulting in loss-of-function phenotypes. The described role of ZIF-1 is to clear PIE-1 and several other CCCH Zn finger proteins from early somatic cells, helping to enrich them in germline precursor cells. Here, we show that proteins tagged with the PIE-1 ZF1 domain are subsequently cleared from primordial germ cells (PGCs) in embryos and from undifferentiated germ cells in larvae and adults by ZIF-1. We harness germline ZIF-1 activity to degrade a ZF1-tagged fusion protein from PGCs and show that its depletion produces phenotypes equivalent to those of a null mutation. Our findings reveal that ZIF-1 transitions from degrading CCCH Zn finger proteins in somatic cells to clearing them from undifferentiated germ cells, and that ZIF-1 activity can be harnessed as a new genetic tool to study the early germline.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Germ Cells/metabolism ; Carrier Proteins/genetics ; Zinc Fingers/genetics
    Chemical Substances Caenorhabditis elegans Proteins ; Carrier Proteins
    Language English
    Publishing date 2023-08-30
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2167-2
    ISSN 1943-2631 ; 0016-6731
    ISSN (online) 1943-2631
    ISSN 0016-6731
    DOI 10.1093/genetics/iyad160
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Niche cells regulate primordial germ cell quiescence in response to basement membrane signaling.

    McIntyre, Daniel C / Nance, Jeremy

    Development (Cambridge, England)

    2023  Volume 150, Issue 16

    Abstract: Stem cell quiescence, proliferation and differentiation are controlled by interactions with niche cells and a specialized extracellular matrix called basement membrane (BM). Direct interactions with adjacent BM are known to regulate stem cell quiescence; ...

    Abstract Stem cell quiescence, proliferation and differentiation are controlled by interactions with niche cells and a specialized extracellular matrix called basement membrane (BM). Direct interactions with adjacent BM are known to regulate stem cell quiescence; however, it is less clear how niche BM relays signals to stem cells that it does not contact. Here, we examine how niche BM regulates Caenorhabditis elegans primordial germ cells (PGCs). BM regulates PGC quiescence even though PGCs are enwrapped by somatic niche cells and do not contact the BM; this can be demonstrated by depleting laminin, which causes normally quiescent embryonic PGCs to proliferate. We show that following laminin depletion, niche cells relay proliferation-inducing signals from the gonadal BM to PGCs via integrin receptors. Disrupting the BM proteoglycan perlecan blocks PGC proliferation when laminin is depleted, indicating that laminin functions to inhibit a proliferation-inducing signal originating from perlecan. Reducing perlecan levels in fed larvae hampers germline growth, suggesting that BM signals regulate germ cell proliferation under physiological conditions. Our results reveal how BM signals can regulate stem cell quiescence indirectly, by activating niche cell integrin receptors.
    MeSH term(s) Animals ; Laminin/metabolism ; Signal Transduction ; Germ Cells/metabolism ; Cell Differentiation ; Basement Membrane/metabolism ; Caenorhabditis elegans/metabolism ; Integrins/metabolism
    Chemical Substances Laminin ; Integrins
    Language English
    Publishing date 2023-08-17
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 90607-4
    ISSN 1477-9129 ; 0950-1991
    ISSN (online) 1477-9129
    ISSN 0950-1991
    DOI 10.1242/dev.201640
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 91: Show issues

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  8. Article ; Online: A polarity pathway for exocyst-dependent intracellular tube extension.

    Abrams, Joshua / Nance, Jeremy

    eLife

    2021  Volume 10

    Abstract: Lumen extension in intracellular tubes can occur when vesicles fuse with an invading apical membrane. Within ... ...

    Abstract Lumen extension in intracellular tubes can occur when vesicles fuse with an invading apical membrane. Within the
    MeSH term(s) Animals ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Polarity ; Cytoplasm/metabolism ; Protein Kinase C/genetics ; Protein Kinase C/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; par-6 protein, C elegans ; PKC-3 protein (EC 2.7.11.13) ; Protein Kinase C (EC 2.7.11.13)
    Language English
    Publishing date 2021-03-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.65169
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  9. Article ; Online: Correction: Independent regulation of mitochondrial DNA quantity and quality in

    Schwartz, Aaron Z A / Tsyba, Nikita / Abdu, Yusuff / Patel, Maulik R / Nance, Jeremy

    eLife

    2023  Volume 12

    Language English
    Publishing date 2023-11-01
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.93941
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  10. Article ; Online: A polarity pathway for exocyst-dependent intracellular tube extension

    Joshua Abrams / Jeremy Nance

    eLife, Vol

    2021  Volume 10

    Abstract: Lumen extension in intracellular tubes can occur when vesicles fuse with an invading apical membrane. Within the Caenorhabditis elegans excretory cell, which forms an intracellular tube, the exocyst vesicle-tethering complex is enriched at the lumenal ... ...

    Abstract Lumen extension in intracellular tubes can occur when vesicles fuse with an invading apical membrane. Within the Caenorhabditis elegans excretory cell, which forms an intracellular tube, the exocyst vesicle-tethering complex is enriched at the lumenal membrane and is required for its outgrowth, suggesting that exocyst-targeted vesicles extend the lumen. Here, we identify a pathway that promotes intracellular tube extension by enriching the exocyst at the lumenal membrane. We show that PAR-6 and PKC-3/aPKC concentrate at the lumenal membrane and promote lumen extension. Using acute protein depletion, we find that PAR-6 is required for exocyst membrane recruitment, whereas PAR-3, which can recruit the exocyst in mammals, appears dispensable for exocyst localization and lumen extension. Finally, we show that CDC-42 and RhoGEF EXC-5/FGD regulate lumen extension by recruiting PAR-6 and PKC-3 to the lumenal membrane. Our findings reveal a pathway that connects CDC-42, PAR proteins, and the exocyst to extend intracellular tubes.
    Keywords polarity ; exocyst ; tubulogenesis ; vesicle trafficking ; PAR proteins ; Rho GTPase ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2021-03-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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