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  1. Article: The two

    Behbehani, Ranya / Johnson, Chloe / Holmes, Alexander J / Gratian, Matthew J / Mulvihill, Daniel P / Buss, Folma

    Frontiers in physiology

    2024  Volume 15, Page(s) 1368054

    Abstract: Myosins of class VI move toward the minus-end of actin filaments and play vital roles in cellular processes such as endocytosis, autophagy, protein secretion, and the regulation of actin filament dynamics. In contrast to the majority of metazoan ... ...

    Abstract Myosins of class VI move toward the minus-end of actin filaments and play vital roles in cellular processes such as endocytosis, autophagy, protein secretion, and the regulation of actin filament dynamics. In contrast to the majority of metazoan organisms examined to date which contain a single MYO6 gene,
    Language English
    Publishing date 2024-04-10
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2024.1368054
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  2. Article ; Online: Unconventional Myosins from

    Johnson, Chloe A / Behbehani, Ranya / Buss, Folma

    Biomolecules

    2022  Volume 12, Issue 12

    Abstract: Unconventional myosins are a superfamily of actin-based motor proteins that perform a number of roles in fundamental cellular processes, including (but not limited to) intracellular trafficking, cell motility, endocytosis, exocytosis and cytokinesis. 40 ... ...

    Abstract Unconventional myosins are a superfamily of actin-based motor proteins that perform a number of roles in fundamental cellular processes, including (but not limited to) intracellular trafficking, cell motility, endocytosis, exocytosis and cytokinesis. 40 myosins genes have been identified in humans, which belong to different 12 classes based on their domain structure and organisation. These genes are widely expressed in different tissues, and mutations leading to loss of function are associated with a wide variety of pathologies while over-expression often results in cancer.
    Language English
    Publishing date 2022-12-16
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom12121889
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  3. Article ; Online: Motor proteins at the mitochondria-cytoskeleton interface.

    Kruppa, Antonina J / Buss, Folma

    Journal of cell science

    2021  Volume 134, Issue 7

    Abstract: Mitochondria are multifunctional organelles that not only produce energy for the cell, but are also important for cell signalling, apoptosis and many biosynthetic pathways. In most cell types, they form highly dynamic networks that are constantly ... ...

    Abstract Mitochondria are multifunctional organelles that not only produce energy for the cell, but are also important for cell signalling, apoptosis and many biosynthetic pathways. In most cell types, they form highly dynamic networks that are constantly remodelled through fission and fusion events, repositioned by motor-dependent transport and degraded when they become dysfunctional. Motor proteins and their tracks are key regulators of mitochondrial homeostasis, and in this Review, we discuss the diverse functions of the three classes of motor proteins associated with mitochondria - the actin-based myosins, as well as the microtubule-based kinesins and dynein. In addition, Miro and TRAK proteins act as adaptors that link kinesin-1 and dynein, as well as myosin of class XIX (MYO19), to mitochondria and coordinate microtubule- and actin-based motor activities. Here, we highlight the roles of motor proteins and motor-linked track dynamics in the transporting and docking of mitochondria, and emphasize their adaptations in specialized cells. Finally, we discuss how motor-cargo complexes mediate changes in mitochondrial morphology through fission and fusion, and how they modulate the turnover of damaged organelles via quality control pathways, such as mitophagy. Understanding the importance of motor proteins for mitochondrial homeostasis will help to elucidate the molecular basis of a number of human diseases.
    MeSH term(s) Cytoskeleton/metabolism ; Dyneins/metabolism ; Humans ; Kinesins/genetics ; Kinesins/metabolism ; Microtubules/metabolism ; Mitochondria/metabolism ; Myosins/metabolism
    Chemical Substances Myo19 protein, human ; Myosins (EC 3.6.4.1) ; Dyneins (EC 3.6.4.2) ; Kinesins (EC 3.6.4.4)
    Language English
    Publishing date 2021-04-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.226084
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  4. Article ; Online: Diverse functions of myosin VI in spermiogenesis.

    Zakrzewski, Przemysław / Lenartowska, Marta / Buss, Folma

    Histochemistry and cell biology

    2021  Volume 155, Issue 3, Page(s) 323–340

    Abstract: Spermiogenesis is the final stage of spermatogenesis, a differentiation process during which unpolarized spermatids undergo excessive remodeling that results in the formation of sperm. The actin cytoskeleton and associated actin-binding proteins play ... ...

    Abstract Spermiogenesis is the final stage of spermatogenesis, a differentiation process during which unpolarized spermatids undergo excessive remodeling that results in the formation of sperm. The actin cytoskeleton and associated actin-binding proteins play crucial roles during this process regulating organelle or vesicle delivery/segregation and forming unique testicular structures involved in spermatid remodeling. In addition, several myosin motor proteins including MYO6 generate force and movement during sperm differentiation. MYO6 is highly unusual as it moves towards the minus end of actin filaments in the opposite direction to other myosin motors. This specialized feature of MYO6 may explain the many proposed functions of this myosin in a wide array of cellular processes in animal cells, including endocytosis, secretion, stabilization of the Golgi complex, and regulation of actin dynamics. These diverse roles of MYO6 are mediated by a range of specialized cargo-adaptor proteins that link this myosin to distinct cellular compartments and processes. During sperm development in a number of different organisms, MYO6 carries out pivotal functions. In Drosophila, the MYO6 ortholog regulates actin reorganization during spermatid individualization and male KO flies are sterile. In C. elegans, the MYO6 ortholog mediates asymmetric segregation of cytosolic material and spermatid budding through cytokinesis, whereas in mice, this myosin regulates assembly of highly specialized actin-rich structures and formation of membrane compartments to allow the formation of fully differentiated sperm. In this review, we will present an overview and compare the diverse function of MYO6 in the specialized adaptations of spermiogenesis in flies, worms, and mammals.
    MeSH term(s) Animals ; Mice ; Myosin Heavy Chains/metabolism ; Spermatogenesis
    Chemical Substances myosin VI ; Myosin Heavy Chains (EC 3.6.4.1)
    Language English
    Publishing date 2021-01-02
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 1222930-1
    ISSN 1432-119X ; 0301-5564 ; 0948-6143
    ISSN (online) 1432-119X
    ISSN 0301-5564 ; 0948-6143
    DOI 10.1007/s00418-020-01954-x
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  5. Article: Approaches to Identify and Characterise MYO6-Cargo Interactions.

    O'Loughlin, Thomas / Kendrick-Jones, John / Buss, Folma

    Advances in experimental medicine and biology

    2020  Volume 1239, Page(s) 355–380

    Abstract: Given the prevalence and importance of the actin cytoskeleton and the host of associated myosin motors, it comes as no surprise to find that they are linked to a plethora of cellular functions and pathologies. Although our understanding of the ... ...

    Abstract Given the prevalence and importance of the actin cytoskeleton and the host of associated myosin motors, it comes as no surprise to find that they are linked to a plethora of cellular functions and pathologies. Although our understanding of the biophysical properties of myosin motors has been aided by the high levels of conservation in their motor domains and the extensive work on myosin in skeletal muscle contraction, our understanding of how the nonmuscle myosins participate in such a wide variety of cellular processes is less clear. It is now well established that the highly variable myosin tails are responsible for targeting these myosins to distinct cellular sites for specific functions, and although a number of adaptor proteins have been identified, our current understanding of the cellular processes involved is rather limited. Furthermore, as more adaptor proteins, cargoes and complexes are identified, the importance of elucidating the regulatory mechanisms involved is essential. Ca
    MeSH term(s) Actin Cytoskeleton ; Adaptor Proteins, Signal Transducing ; Humans ; Myosin Heavy Chains/metabolism ; Protein Binding
    Chemical Substances Adaptor Proteins, Signal Transducing ; myosin VI ; Myosin Heavy Chains (EC 3.6.4.1)
    Language English
    Publishing date 2020-05-22
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 410187-X
    ISSN 0065-2598
    ISSN 0065-2598
    DOI 10.1007/978-3-030-38062-5_15
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    Einzelsignatur: Show issues

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  6. Article ; Online: Actin cages isolate damaged mitochondria during mitophagy.

    Kruppa, Antonina J / Buss, Folma

    Autophagy

    2018  Volume 14, Issue 9, Page(s) 1644–1645

    Abstract: Mitochondrial homeostasis is maintained by removing dysfunctional, ubiquitinated mitochondria from the network via PRKN-dependent mitophagy. MYO6, a unique myosin that moves towards the minus ends of actin filaments, forms a complex with PRKN and is ... ...

    Abstract Mitochondrial homeostasis is maintained by removing dysfunctional, ubiquitinated mitochondria from the network via PRKN-dependent mitophagy. MYO6, a unique myosin that moves towards the minus ends of actin filaments, forms a complex with PRKN and is selectively recruited to damaged mitochondria by binding to ubiquitin. On the mitochondrial surface, this myosin motor initiates the assembly of F-actin cages, which serve as a quality control mechanism to isolate dysfunctional mitochondria thereby preventing their refusion with neighboring populations. MYO6 also plays a role in the later stages of the mitophagy pathway by tethering endosomes to actin filaments facilitating mitophagosome maturation and autophagosome-lysosome fusion.
    MeSH term(s) Actins ; Autophagy ; HeLa Cells ; Humans ; Mitochondria ; Mitophagy ; Myosin Heavy Chains ; Ubiquitin-Protein Ligases
    Chemical Substances Actins ; myosin VI ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Myosin Heavy Chains (EC 3.6.4.1)
    Language English
    Publishing date 2018-07-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2018.1486152
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    Zs.A 6741: Show issues Location:
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  7. Article ; Online: Editorial: The Role of Optineurin in Immunity and Immune-Mediated Diseases.

    Smith, Andrew M / Buss, Folma / Munitic, Ivana

    Frontiers in immunology

    2019  Volume 10, Page(s) 2803

    MeSH term(s) Autophagy ; Cell Cycle Proteins/immunology ; Cell Death ; Humans ; Immune System Diseases/immunology ; Membrane Transport Proteins/immunology ; Signal Transduction
    Chemical Substances Cell Cycle Proteins ; Membrane Transport Proteins ; OPTN protein, human
    Language English
    Publishing date 2019-12-11
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2019.02803
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  8. Article ; Online: Ultrastructural insights into pathogen clearance by autophagy.

    Kishi-Itakura, Chieko / Ktistakis, Nicholas T / Buss, Folma

    Traffic (Copenhagen, Denmark)

    2020  Volume 21, Issue 4, Page(s) 310–323

    Abstract: Autophagy defends cells against proliferation of bacteria such as Salmonella in the cytosol. After escape from a damaged Salmonella-containing vacuole (SCV) exposing luminal glycans that bind to Galectin-8, the host cell ubiquitination machinery deposits ...

    Abstract Autophagy defends cells against proliferation of bacteria such as Salmonella in the cytosol. After escape from a damaged Salmonella-containing vacuole (SCV) exposing luminal glycans that bind to Galectin-8, the host cell ubiquitination machinery deposits a dense layer of ubiquitin around the cytosolic bacteria. The nature and spatial distribution of this ubiquitin coat in relation to other autophagy-related membranes are unknown. Using transmission electron microscopy, we determined the exact localisation of ubiquitin, the ruptured SCV membrane and phagophores around cytosolic Salmonella. Ubiquitin was not predominantly present on the Salmonella surface, but enriched on the fragmented SCV. Cytosolic bacteria without SCVs were less efficiently targeted by phagophores. Single bacteria were contained in single phagophores but multiple bacteria could be within large autophagic vacuoles reaching 30 μm in circumference. These large phagophores followed the contour of the engulfed bacteria, they were frequently in close association with endoplasmic reticulum membranes and, within them, remnants of the SCV were seen associated with each engulfed particle. Our data suggest that the Salmonella SCV has a major role in the formation of autophagic phagophores and highlight evolutionary conserved parallel mechanisms between xenophagy and mitophagy with the fragmented SCV and the damaged outer mitochondrial membrane serving similar functions.
    MeSH term(s) Autophagosomes/metabolism ; Autophagy ; Microscopy, Electron, Transmission ; Salmonella typhimurium/metabolism ; Ubiquitin/metabolism ; Ubiquitination ; Vacuoles/metabolism
    Chemical Substances Ubiquitin
    Language English
    Publishing date 2020-03-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12723
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  9. Article ; Online: Editorial Overview: Myosins in Review.

    Kendrick-Jones, John / Buss, Folma

    Traffic (Copenhagen, Denmark)

    2016  Volume 17, Issue 8, Page(s) 819–821

    MeSH term(s) Animals ; Humans ; Myosins/chemistry ; Myosins/classification ; Myosins/genetics ; Myosins/metabolism
    Chemical Substances Myosins (EC 3.6.4.1)
    Language English
    Publishing date 2016-05-24
    Publishing country England
    Document type Editorial ; Introductory Journal Article
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12405
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  10. Article ; Online: The Use of Correlative Light-Electron Microscopy (CLEM) to Study PINK1/Parkin-Mediated Mitophagy.

    Kishi-Itakura, Chieko / Buss, Folma

    Methods in molecular biology (Clifton, N.J.)

    2017  Volume 1759, Page(s) 29–39

    Abstract: In this chapter we describe the use of correlative light-electron microscopy (CLEM) to study, in cultured cells, the turnover of damaged mitochondria by PINK1/Parkin-dependent mitophagy. CLEM combines the advantages of light microscopy, which allows to ... ...

    Abstract In this chapter we describe the use of correlative light-electron microscopy (CLEM) to study, in cultured cells, the turnover of damaged mitochondria by PINK1/Parkin-dependent mitophagy. CLEM combines the advantages of light microscopy, which allows to image and rapidly screen a large number of the cells, while electron microscopy provides high-resolution imaging of these selected cells and a detailed structural analysis of their cellular organelles. We describe in detail how to prepare the cell cultures for optimum preservation of their cellular ultrastructure for CLEM using the most suitable buffers, fixatives, and embedding resins. These protocols are applicable for detailed ultrastructural analysis in a wide variety of organisms and cells, ranging from prokaryotic bacteria to mammalian cells.
    MeSH term(s) Animals ; Cell Line ; Humans ; Mice ; Microscopy, Electron ; Microscopy, Fluorescence ; Mitochondria/physiology ; Mitochondria/ultrastructure ; Mitophagy ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27) ; Protein Kinases (EC 2.7.-) ; PTEN-induced putative kinase (EC 2.7.11.1)
    Language English
    Publishing date 2017-03-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/7651_2017_8
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