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  1. AU="Vines, James H"
  2. AU="Prada, Andrés"
  3. AU="Chong, Eui Hyuk"
  4. AU="Daisuke Nakamura"
  5. AU="Forrester, Lewis"
  6. AU="Soares-Freitas, Rosana Aparecida M"
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  12. AU="Thete, Raghavendra"
  13. AU="Sayed, El-Sayed T A"
  14. AU="Lezrek, Mohamed"
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  1. Article ; Online: The endocytic pathways of Dictyostelium discoideum.

    Vines, James H / King, Jason S

    The International journal of developmental biology

    2019  Volume 63, Issue 8-9-10, Page(s) 461–471

    Abstract: The formation and processing of vesicles from the cell surface serves many important cellular functions ranging from nutrient acquisition to regulating the turnover of membrane components and signalling. In this article, we summarise the endocytic ... ...

    Abstract The formation and processing of vesicles from the cell surface serves many important cellular functions ranging from nutrient acquisition to regulating the turnover of membrane components and signalling. In this article, we summarise the endocytic pathways of the social amoeba Dictyostelium from the clathrin-dependent and independent internalisation of surface components to the engulfment of bacteria or fluid by phagocytosis and macropinocytosis respectively. Due to similarities with the professional phagocytes of the mammalian immune system Dictyostelium has been extensively used to investigate the complex remodelling and trafficking events that occur as phagosomes and macropinosomes transit through the cell. Here we discuss what is known about this maturation process in order to kill any potential pathogens and obtain nutrients for growth. Finally, we aim to put these studies in evolutionary context and highlight some of the many questions that remain in our understanding of these complex and important pathways.
    MeSH term(s) Cell Membrane/metabolism ; Cell Movement ; Clathrin/metabolism ; Dictyostelium/physiology ; Endocytosis ; Exocytosis ; Immune System ; Lysosomes/metabolism ; Phagocytosis ; Phagosomes/metabolism ; Pinocytosis ; Signal Transduction
    Chemical Substances Clathrin
    Language English
    Publishing date 2019-12-12
    Publishing country Spain
    Document type Journal Article ; Review
    ZDB-ID 1036070-0
    ISSN 1696-3547 ; 0214-6282
    ISSN (online) 1696-3547
    ISSN 0214-6282
    DOI 10.1387/ijdb.190236jk
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Recombinant biosensors for multiplex and super-resolution imaging of phosphoinositides.

    Maib, Hannes / Adarska, Petia / Hunton, Robert / Vines, James H / Strutt, David / Bottanelli, Francesca / Murray, David H

    The Journal of cell biology

    2024  Volume 223, Issue 6

    Abstract: Phosphoinositides are a small family of phospholipids that act as signaling hubs and key regulators of cellular function. Detecting their subcellular distribution is crucial to gain insights into membrane organization and is commonly done by the ... ...

    Abstract Phosphoinositides are a small family of phospholipids that act as signaling hubs and key regulators of cellular function. Detecting their subcellular distribution is crucial to gain insights into membrane organization and is commonly done by the overexpression of biosensors. However, this leads to cellular perturbations and is challenging in systems that cannot be transfected. Here, we present a toolkit for the reliable, fast, multiplex, and super-resolution detection of phosphoinositides in fixed cells and tissue, based on recombinant biosensors with self-labeling SNAP tags. These are highly specific and reliably visualize the subcellular distributions of phosphoinositides across scales, from 2D or 3D cell culture to Drosophila tissue. Further, these probes enable super-resolution approaches, and using STED microscopy, we reveal the nanoscale organization of PI(3)P on endosomes and PI(4)P on the Golgi. Finally, multiplex staining reveals an unexpected presence of PI(3,5)P2-positive membranes in swollen lysosomes following PIKfyve inhibition. This approach enables the versatile, high-resolution visualization of multiple phosphoinositide species in an unprecedented manner.
    MeSH term(s) Endosomes/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphatidylinositols/chemistry ; Phosphatidylinositols/metabolism ; Biosensing Techniques/methods
    Chemical Substances phosphatidylinositol 3-phosphate ; Phosphatidylinositol Phosphates ; Phosphatidylinositols
    Language English
    Publishing date 2024-04-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202310095
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: A PI(3,5)P2 reporter reveals PIKfyve activity and dynamics on macropinosomes and phagosomes.

    Vines, James H / Maib, Hannes / Buckley, Catherine M / Gueho, Aurelie / Zhu, Zhou / Soldati, Thierry / Murray, David H / King, Jason S

    The Journal of cell biology

    2023  Volume 222, Issue 9

    Abstract: Phosphoinositide signaling lipids (PIPs) are key regulators of membrane identity and trafficking. Of these, PI(3,5)P2 is one of the least well-understood, despite key roles in many endocytic pathways including phagocytosis and macropinocytosis. PI(3,5)P2 ...

    Abstract Phosphoinositide signaling lipids (PIPs) are key regulators of membrane identity and trafficking. Of these, PI(3,5)P2 is one of the least well-understood, despite key roles in many endocytic pathways including phagocytosis and macropinocytosis. PI(3,5)P2 is generated by the phosphoinositide 5-kinase PIKfyve, which is critical for phagosomal digestion and antimicrobial activity. However PI(3,5)P2 dynamics and regulation remain unclear due to lack of reliable reporters. Using the amoeba Dictyostelium discoideum, we identify SnxA as a highly selective PI(3,5)P2-binding protein and characterize its use as a reporter for PI(3,5)P2 in both Dictyostelium and mammalian cells. Using GFP-SnxA, we demonstrate that Dictyostelium phagosomes and macropinosomes accumulate PI(3,5)P2 3 min after engulfment but are then retained differently, indicating pathway-specific regulation. We further find that PIKfyve recruitment and activity are separable and that PIKfyve activation stimulates its own dissociation. SnxA is therefore a new tool for reporting PI(3,5)P2 in live cells that reveals key mechanistic details of the role and regulation of PIKfyve/PI(3,5)P2.
    MeSH term(s) Animals ; Dictyostelium/genetics ; Endosomes ; Mammals ; Phagosomes ; Phosphatidylinositols ; Phosphatidylinositol 3-Kinases/metabolism
    Chemical Substances phosphatidylinositol 3,5-diphosphate ; Phosphatidylinositols ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
    Language English
    Publishing date 2023-06-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202209077
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Phosphatidylinositol 3,5-bisphosphate facilitates axonal vesicle transport and presynapse assembly.

    Rizalar, Filiz Sila / Lucht, Max T / Petzoldt, Astrid / Kong, Shuhan / Sun, Jiachen / Vines, James H / Telugu, Narasimha Swamy / Diecke, Sebastian / Kaas, Thomas / Bullmann, Torsten / Schmied, Christopher / Löwe, Delia / King, Jason S / Cho, Wonhwa / Hallermann, Stefan / Puchkov, Dmytro / Sigrist, Stephan J / Haucke, Volker

    Science (New York, N.Y.)

    2023  Volume 382, Issue 6667, Page(s) 223–230

    Abstract: Neurons relay information via specialized presynaptic compartments for neurotransmission. Unlike conventional organelles, the specialized apparatus characterizing the neuronal presynapse must form de novo. How the components for presynaptic ... ...

    Abstract Neurons relay information via specialized presynaptic compartments for neurotransmission. Unlike conventional organelles, the specialized apparatus characterizing the neuronal presynapse must form de novo. How the components for presynaptic neurotransmission are transported and assembled is poorly understood. Our results show that the rare late endosomal signaling lipid phosphatidylinositol 3,5-bisphosphate [PI(3,5)P
    MeSH term(s) Humans ; Axonal Transport/physiology ; Kinesins/metabolism ; Neurons/metabolism ; Synaptic Vesicles/metabolism ; Phosphatidylinositol Phosphates/metabolism
    Chemical Substances KIF1A protein, human ; Kinesins (EC 3.6.4.4) ; phosphatidylinositol 3,5-diphosphate ; Phosphatidylinositol Phosphates
    Language English
    Publishing date 2023-10-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.adg1075
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Coordinated Ras and Rac Activity Shapes Macropinocytic Cups and Enables Phagocytosis of Geometrically Diverse Bacteria.

    Buckley, Catherine M / Pots, Henderikus / Gueho, Aurelie / Vines, James H / Munn, Christopher J / Phillips, Ben A / Gilsbach, Bernd / Traynor, David / Nikolaev, Anton / Soldati, Thierry / Parnell, Andrew J / Kortholt, Arjan / King, Jason S

    Current biology : CB

    2020  Volume 30, Issue 15, Page(s) 2912–2926.e5

    Abstract: Engulfment of extracellular material by phagocytosis or macropinocytosis depends on the ability of cells to generate specialized cup-shaped protrusions. To effectively capture and internalize their targets, these cups are organized into a ring or ruffle ... ...

    Abstract Engulfment of extracellular material by phagocytosis or macropinocytosis depends on the ability of cells to generate specialized cup-shaped protrusions. To effectively capture and internalize their targets, these cups are organized into a ring or ruffle of actin-driven protrusion encircling a non-protrusive interior domain. These functional domains depend on the combined activities of multiple Ras and Rho family small GTPases, but how their activities are integrated and differentially regulated over space and time is unknown. Here, we show that the amoeba Dictyostelium discoideum coordinates Ras and Rac activity using the multidomain protein RGBARG (RCC1, RhoGEF, BAR, and RasGAP-containing protein). We find RGBARG uses a tripartite mechanism of Ras, Rac, and phospholipid interactions to localize at the protruding edge and interface with the interior of both macropinocytic and phagocytic cups. There, we propose RGBARG shapes the protrusion by expanding Rac activation at the rim while suppressing expansion of the active Ras interior domain. Consequently, cells lacking RGBARG form enlarged, flat interior domains unable to generate large macropinosomes. During phagocytosis, we find that disruption of RGBARG causes a geometry-specific defect in engulfing rod-shaped bacteria and ellipsoidal beads. This demonstrates the importance of coordinating small GTPase activities during engulfment of more complex shapes and thus the full physiological range of microbes, and how this is achieved in a model professional phagocyte.
    MeSH term(s) Bacteria ; Cell Cycle Proteins ; Dictyostelium/cytology ; Dictyostelium/immunology ; Dictyostelium/metabolism ; Dictyostelium/physiology ; Phagocytosis ; Pinocytosis ; rac GTP-Binding Proteins/metabolism ; ras Proteins/metabolism
    Chemical Substances Cell Cycle Proteins ; rac GTP-Binding Proteins (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2020-06-11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2020.05.049
    Database MEDical Literature Analysis and Retrieval System OnLINE

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