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Cover image for Vol. 15 Issue 5

Edited By: Michael S. Marks, Mark C. P. Marsh, Trina A. Schroer, Tom H. Stevens

Online ISSN: 1600-0854

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  • TOOLBOX: High-Throughput Quantitation of Intracellular Trafficking and Organelle Disruption by Flow Cytometry

    TOOLBOX: High-Throughput Quantitation of Intracellular Trafficking and Organelle Disruption by Flow Cytometry

    A flow chart for the monitoring of cargo trafficking by pulse-width analysis. Shown is the protocol for the monitoring cargo trafficking from the plasma membrane to intracellular compartments by pulse-width analysis.

  • ORIGINAL ARTICLE: A Dynamin Homolog Promotes the Transition from Hemifusion to Content Mixing in Intracellular Membrane Fusion

    ORIGINAL ARTICLE: A Dynamin Homolog Promotes the Transition from Hemifusion to Content Mixing in Intracellular Membrane Fusion

    Schematic representation of Vps1 function inSNARE-mediated fusion.

  • ORIGINAL ARTICLE: Yeast Endocytic Adaptor AP-2 Binds the Stress Sensor Mid2 and Functions in Polarized Cell Responses

    ORIGINAL ARTICLE: Yeast Endocytic Adaptor AP-2 Binds the Stress Sensor Mid2 and Functions in Polarized Cell Responses

    Defects in polarity of cell wall markers inapm4Δ cells. A) Cells were incubated with concanavalin A conjugated to distinct fluorophores to label old and new growth of cells. Left panels show representative wild type cells; right panels show labelled apm4 null cells. Scale bar = 5 µm. B) Wild type and apm4Δ cells were induced to express GFP-Cdc42 by growth in galactose containing medium for 3 h before addition of alpha factor for 2 h. Localization of GFP-Cdc42 was analysed in 100 cells in three independent experiments. Scale bar = 5 µm. C) Pkc1-GFP was analysed in cells to determine localization under conditions of vegetative growth. Scale bar = 5 µm. Shown are cells from different stages of budding. D) Localization of Pkc1-GFP was analysed in cells and extent of polarity recorded and shown graphically. Data are from three independent experiments with >100 cells counted in each experiment.

  • ORIGINAL ARTICLE: Regulated Oligomerization Induces Uptake of a Membrane Protein into COPII Vesicles Independent of Its Cytosolic Tail

    ORIGINAL ARTICLE: Regulated Oligomerization Induces Uptake of a Membrane Protein into COPII Vesicles Independent of Its Cytosolic Tail

    One hypothetic model: FT-FFinfluences membrane bending upon dimerization. A) FT-FF is randomly inserted into the ER membrane in type I and type II orientation (lower and faster mobility species in the gels, respectively, see, e.g. Figure ). B and C) Addition of the dimerizer AP20187 results in polymerization of the respective FT-FF species. We hypothesize a complex conformation that strongly imparts membrane bending (depicted as triangular FKBP domains): The type II-oriented oligomer favors a concave membrane curvature opposing vesicle generation (B), whereas the type I-oriented oligomer induces convex membrane bending thereby facilitating COPII vesicle formation (C). HA2 tag and glycans of the protein construct are omitted for clarity.

  • ORIGINAL ARTICLE: Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins

    ORIGINAL ARTICLE: Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins

    Structure ofSidCNT(residues 1-608). A) SidCNT, colored from blue at the N-terminus to red at the C-terminus. The domains are labeled A–C. B) Secondary structure topology of SidCNT. C) Sequence alignment of SidC and SdcA. D) HEK293 cells stably expressing 3XFlag-tagged Rab1 were transfected with the cDNAs encoding 3XFLAG-tagged SdcA full-length (3XFLAG-SdcAFL) or SdcA lacking residues 221-329 (3XFLAG-SdcAΔC); 14 h after transfection, cells were infected with a L. pneumophilaWT strain or ΔsdcA-sidC strain for 1 h, following which they were lysed. Rab1A was immunoprecipitated using FLAG antibody-coated beads. After incubation, beads were boiled and subjected to SDS–PAGE analysis and subsequently probed with either a Rab1A-specific antibody or a FLAG antibody. E) Model of SdcA/SidC-mediated vesicle tethering at the LCV.

  • REVIEW: The Cellular and Physiological Functions of the Lowe Syndrome Protein OCRL1

    REVIEW: The Cellular and Physiological Functions of the Lowe Syndrome Protein OCRL1

    Cellular localization ofOCRL1. A) OCRL1 (blue hexagons) has been localized to a number of cellular compartments. It is present at the TGN and various compartments of the endocytic pathway, where it resides at late-stage clathrin-coated pits, clathrin-coated vesicles, signaling endosomes, early or sorting endosomes and on recycling endosomes. OCRL1 has also been localized to the basal body of primary cilia, and it may also localize to the cilium itself. In maturing epithelia, OCRL1 transiently localizes to adherens and tight junctions. OCRL1 is recruited to phagosomes at a late stage in their formation, and is important for closure of the phagocytic cup as well as signaling events that occur post-sealing. OCRL1 is recruited to phagosomes generated by invading pathogenic bacteria such as Yersinia or Listeria, and has also been localized on intracellular inclusions generated by certain bacteria, e.g. Legionella or Chlamydia. B) OCRL1 localizes to the midbody in cells undergoing cytokinesis. C) OCRL1 has been localized to the lamellipodia of migrating fibroblasts.

  • TOOLBOX: High-Throughput Quantitation of Intracellular Trafficking and Organelle Disruption by Flow Cytometry
  • ORIGINAL ARTICLE: A Dynamin Homolog Promotes the Transition from Hemifusion to Content Mixing in Intracellular Membrane Fusion
  • ORIGINAL ARTICLE: Yeast Endocytic Adaptor AP-2 Binds the Stress Sensor Mid2 and Functions in Polarized Cell Responses
  • ORIGINAL ARTICLE: Regulated Oligomerization Induces Uptake of a Membrane Protein into COPII Vesicles Independent of Its Cytosolic Tail
  • ORIGINAL ARTICLE: Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins
  • REVIEW: The Cellular and Physiological Functions of the Lowe Syndrome Protein OCRL1

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Regulated Oligomerization Induces Uptake of a Membrane Protein into COPII Vesicles Independent of Its Cytosolic Tail
Sebastian Springer, Per Malkus, Britta Borchert, Ursula Wellbrock, Rainer Duden and Randy Schekman

Using a model transmembrane fusion protein, Springer et al. demonstrate that induction of oligomerization stimulates its ER export. The authors propose that oligomerization induces local membrane bending, which promotes COPII vesicle generation.

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