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  1. Article ; Online: Flagging fusion: Phosphatidylserine signaling in cell-cell fusion.

    Whitlock, Jarred M / Chernomordik, Leonid V

    The Journal of biological chemistry

    2021  Volume 296, Page(s) 100411

    Abstract: Formations of myofibers, osteoclasts, syncytiotrophoblasts, and fertilized zygotes share a common step, cell-cell fusion. Recent years have brought about considerable progress in identifying some of the proteins involved in these and other cell-fusion ... ...

    Abstract Formations of myofibers, osteoclasts, syncytiotrophoblasts, and fertilized zygotes share a common step, cell-cell fusion. Recent years have brought about considerable progress in identifying some of the proteins involved in these and other cell-fusion processes. However, even for the best-characterized cell fusions, we still do not know the mechanisms that regulate the timing of cell-fusion events. Are they fully controlled by the expression of fusogenic proteins or do they also depend on some triggering signal that activates these proteins? The latter scenario would be analogous to the mechanisms that control the timing of exocytosis initiated by Ca
    MeSH term(s) Cell Fusion ; Exocytosis ; Humans ; Phosphatidylserines/metabolism ; Signal Transduction ; Virus Internalization
    Chemical Substances Phosphatidylserines
    Language English
    Publishing date 2021-02-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2021.100411
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  2. Article ; Online: An inducible explant model of osteoclast-osteoprogenitor coordination in exacerbated osteoclastogenesis.

    Whitlock, Jarred M / de Castro, Luis F / Collins, Michael T / Chernomordik, Leonid V / Boyce, Alison M

    iScience

    2023  Volume 26, Issue 4, Page(s) 106470

    Abstract: Elucidating a basic blueprint of osteoclast-osteoblast coordination in skeletal remodeling and understanding how this coordination breaks down with age and disease is essential for addressing the growing skeletal health problem in our aging population. ... ...

    Abstract Elucidating a basic blueprint of osteoclast-osteoblast coordination in skeletal remodeling and understanding how this coordination breaks down with age and disease is essential for addressing the growing skeletal health problem in our aging population. The paucity of simple, activatable, biologically relevant models of osteoclast-osteoblast coordination has hindered our understanding of how skeletal remolding is regulated. Here, we describe an inducible
    Language English
    Publishing date 2023-03-23
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2023.106470
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  3. Article: RANKL inhibition reduces lesional cellularity and Gα

    de Castro, Luis F / Whitlock, Jarred M / Michel, Zachary / Pan, Kristen / Taylor, Jocelyn / Szymczuk, Vivian / Boyce, Brendan / Martin, Daniel / Kram, Vardit / Galisteo, Rebeca / Melikov, Kamran / Chernomordik, Leonid V / Collins, Michael T / Boyce, Alison M

    Bone research

    2024  Volume 12, Issue 1, Page(s) 10

    Abstract: Fibrous dysplasia (FD) is a rare, disabling skeletal disease for which there are no established treatments. Growing evidence supports inhibiting the osteoclastogenic factor receptor activator of nuclear kappa-B ligand (RANKL) as a potential treatment ... ...

    Abstract Fibrous dysplasia (FD) is a rare, disabling skeletal disease for which there are no established treatments. Growing evidence supports inhibiting the osteoclastogenic factor receptor activator of nuclear kappa-B ligand (RANKL) as a potential treatment strategy. In this study, we investigated the mechanisms underlying RANKL inhibition in FD tissue and its likely indirect effects on osteoprogenitors by evaluating human FD tissue pre- and post-treatment in a phase 2 clinical trial of denosumab (NCT03571191) and in murine in vivo and ex vivo preclinical models. Histological analysis of human and mouse tissue demonstrated increased osteogenic maturation, reduced cellularity, and reduced expression of the pathogenic Gα
    MeSH term(s) Animals ; Humans ; Mice ; Denosumab/pharmacology ; Fibrous Dysplasia of Bone/drug therapy ; Ligands ; Osteoblasts/metabolism ; Osteogenesis/genetics
    Chemical Substances Denosumab (4EQZ6YO2HI) ; Ligands
    Language English
    Publishing date 2024-02-20
    Publishing country China
    Document type Clinical Trial, Phase II ; Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2803313-9
    ISSN 2095-6231 ; 2095-4700
    ISSN (online) 2095-6231
    ISSN 2095-4700
    DOI 10.1038/s41413-023-00311-7
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  4. Article ; Online: Membrane fusion: Conserved and diverse.

    Podbilewicz, Benjamin / Chernomordik, Leonid V

    Seminars in cell & developmental biology

    2016  Volume 60, Page(s) 63–64

    Language English
    Publishing date 2016-12
    Publishing country England
    Document type Editorial
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2016.11.009
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    Zs.A 2918: Show issues Location:
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  5. Article ; Online: Cell surface-bound La protein regulates the cell fusion stage of osteoclastogenesis.

    Whitlock, Jarred M / Leikina, Evgenia / Melikov, Kamran / De Castro, Luis Fernandez / Mattijssen, Sandy / Maraia, Richard J / Collins, Michael T / Chernomordik, Leonid V

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 616

    Abstract: Multinucleated osteoclasts, essential for skeletal remodeling in health and disease, are formed by the fusion of osteoclast precursors, where each fusion event raises their bone-resorbing activity. Here we show that the nuclear RNA chaperone, La protein ... ...

    Abstract Multinucleated osteoclasts, essential for skeletal remodeling in health and disease, are formed by the fusion of osteoclast precursors, where each fusion event raises their bone-resorbing activity. Here we show that the nuclear RNA chaperone, La protein has an additional function as an osteoclast fusion regulator. Monocyte-to-osteoclast differentiation starts with a drastic decrease in La levels. As fusion begins, La reappears as a low molecular weight species at the osteoclast surface, where it promotes fusion. La's role in promoting osteoclast fusion is independent of canonical La-RNA interactions and involves direct interactions between La and Annexin A5, which anchors La to transiently exposed phosphatidylserine at the surface of fusing osteoclasts. Disappearance of cell-surface La, and the return of full length La to the nuclei of mature, multinucleated osteoclasts, acts as an off switch of their fusion activity. Targeting surface La in a novel explant model of fibrous dysplasia inhibits excessive osteoclast formation characteristic of this disease, highlighting La's potential as a therapeutic target.
    MeSH term(s) Humans ; Bone Resorption/metabolism ; Cell Differentiation ; Cell Fusion ; Cell Membrane/metabolism ; Membrane Proteins/metabolism ; Osteoclasts/metabolism ; Osteogenesis
    Chemical Substances Membrane Proteins ; La protein, human
    Language English
    Publishing date 2023-02-04
    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/s41467-023-36168-x
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  6. Article ; Online: An inducible explant model of osteoclast-osteoprogenitor coordination in exacerbated osteoclastogenesis

    Jarred M. Whitlock / Luis F. de Castro / Michael T. Collins / Leonid V. Chernomordik / Alison M. Boyce

    iScience, Vol 26, Iss 4, Pp 106470- (2023)

    2023  

    Abstract: Summary: Elucidating a basic blueprint of osteoclast-osteoblast coordination in skeletal remodeling and understanding how this coordination breaks down with age and disease is essential for addressing the growing skeletal health problem in our aging ... ...

    Abstract Summary: Elucidating a basic blueprint of osteoclast-osteoblast coordination in skeletal remodeling and understanding how this coordination breaks down with age and disease is essential for addressing the growing skeletal health problem in our aging population. The paucity of simple, activatable, biologically relevant models of osteoclast-osteoblast coordination has hindered our understanding of how skeletal remolding is regulated. Here, we describe an inducible ex vivo model of osteoclast-osteoblast progenitor coordination. Induction activates the release of osteoclastogenic factors from osteoprogenitors, which elicits the differentiation and fusion of neighboring preosteoclasts. In turn, multinucleated osteoclasts release soluble coupling factors, RANK+ extracellular vesicles and promote osteoprogenitor proliferation, recapitulating aspects of perturbed coordination in diseases underpinned by excessive osteoclast formation. We expect this model to expedite the investigation of cell-cell fusion, osteoclast-osteoblast progenitor coordination, and extracellular vesicle signaling during bone remodeling and offer a powerful tool for evaluating signaling cascades and novel therapeutic interventions in osteoclast-linked skeletal disease.
    Keywords Biological sciences ; Cell biology ; Stem cells research ; Science ; Q
    Language English
    Publishing date 2023-04-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: An improved metrics for osteoclast multinucleation.

    Verma, Santosh K / Chernomordik, Leonid V / Melikov, Kamran

    Scientific reports

    2018  Volume 8, Issue 1, Page(s) 1768

    Abstract: Cell-cell fusion is a key stage in development and maintenance of multinucleated cells that resorb bones and form our skeletal muscles and placenta. Here, we focus on osteoclast formation to suggest new ways of unbiased presentation of cell fusion at ... ...

    Abstract Cell-cell fusion is a key stage in development and maintenance of multinucleated cells that resorb bones and form our skeletal muscles and placenta. Here, we focus on osteoclast formation to suggest new ways of unbiased presentation of cell fusion at given conditions that combine empirical cumulative distribution function for the sizes of multinucleated cells with the total number of cell-cell fusion events, which generate these cells.
    MeSH term(s) Animals ; Bone Resorption/physiopathology ; Bone and Bones/physiology ; Cell Differentiation/physiology ; Cell Fusion/methods ; Cells, Cultured ; Humans ; Mice ; Osteoclasts/physiology ; RAW 264.7 Cells
    Language English
    Publishing date 2018-01-29
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-018-20031-x
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  8. Article ; Online: Myoblast fusion: playing hard to get.

    Chernomordik, Leonid V / Kozlov, Michael M

    Developmental cell

    2015  Volume 32, Issue 5, Page(s) 529–530

    Abstract: In Drosophila myoblast fusion, the fusing cell invades another by actin-enriched protrusion. In this issue of Developmental Cell, Kim et al. (2015) examine the myoblast fusion mechanism from the perspective of the "receiving" cell and report that fusion ... ...

    Abstract In Drosophila myoblast fusion, the fusing cell invades another by actin-enriched protrusion. In this issue of Developmental Cell, Kim et al. (2015) examine the myoblast fusion mechanism from the perspective of the "receiving" cell and report that fusion depends on the ability of this cell to stiffen its actomyosin cortex.
    MeSH term(s) Animals ; Cell Membrane/metabolism ; Drosophila melanogaster/metabolism ; Mechanotransduction, Cellular ; Membrane Fusion/physiology ; Myosin Type II/metabolism
    Chemical Substances Myosin Type II (EC 3.6.1.-)
    Language English
    Publishing date 2015-02-11
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2015.02.018
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    Zs.A 5742: Show issues Location:
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  9. Article ; Online: Membrane tension and membrane fusion.

    Kozlov, Michael M / Chernomordik, Leonid V

    Current opinion in structural biology

    2015  Volume 33, Page(s) 61–67

    Abstract: Diverse cell biological processes that involve shaping and remodeling of cell membranes are regulated by membrane lateral tension. Here we focus on the role of tension in driving membrane fusion. We discuss the physics of membrane tension, forces that ... ...

    Abstract Diverse cell biological processes that involve shaping and remodeling of cell membranes are regulated by membrane lateral tension. Here we focus on the role of tension in driving membrane fusion. We discuss the physics of membrane tension, forces that can generate the tension in plasma membrane of a cell, and the hypothesis that tension powers expansion of membrane fusion pores in late stages of cell-to-cell and exocytotic fusion. We propose that fusion pore expansion can require unusually large membrane tensions or, alternatively, low line tensions of the pore resulting from accumulation in the pore rim of membrane-bending proteins. Increase of the inter-membrane distance facilitates the reaction.
    MeSH term(s) Cell Adhesion ; Cell Membrane/physiology ; Membrane Fusion ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Osmosis
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2015-08-15
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2015.07.010
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  10. Article ; Online: How cells fuse.

    Brukman, Nicolas G / Uygur, Berna / Podbilewicz, Benjamin / Chernomordik, Leonid V

    The Journal of cell biology

    2019  Volume 218, Issue 5, Page(s) 1436–1451

    Abstract: Cell-cell fusion remains the least understood type of membrane fusion process. However, the last few years have brought about major advances in understanding fusion between gametes, myoblasts, macrophages, trophoblasts, epithelial, cancer, and other ... ...

    Abstract Cell-cell fusion remains the least understood type of membrane fusion process. However, the last few years have brought about major advances in understanding fusion between gametes, myoblasts, macrophages, trophoblasts, epithelial, cancer, and other cells in normal development and in diseases. While different cell fusion processes appear to proceed via similar membrane rearrangements, proteins that have been identified as necessary and sufficient for cell fusion (fusogens) use diverse mechanisms. Some fusions are controlled by a single fusogen; other fusions depend on several proteins that either work together throughout the fusion pathway or drive distinct stages. Furthermore, some fusions require fusogens to be present on both fusing membranes, and in other fusions, fusogens have to be on only one of the membranes. Remarkably, some of the proteins that fuse cells also sculpt single cells, repair neurons, promote scission of endocytic vesicles, and seal phagosomes. In this review, we discuss the properties and diversity of the known proteins mediating cell-cell fusion and highlight their different working mechanisms in various contexts.
    MeSH term(s) Animals ; Cell Fusion ; Cell Membrane/metabolism ; Humans ; Membrane Fusion ; Membrane Proteins/metabolism
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2019-04-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201901017
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