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Cover image for Vol. 15 Issue 5

May 2014

Volume 15, Issue 5

Pages i–i, 471–582

  1. Issue Information

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    2. Issue Information
    3. Review
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      Issue Information (page i)

      Version of Record online: 4 APR 2014 | DOI: 10.1111/tra.12107

  2. Review

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    2. Issue Information
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      The Cellular and Physiological Functions of the Lowe Syndrome Protein OCRL1 (pages 471–487)

      Zenobia B. Mehta, Grzegorz Pietka and Martin Lowe

      Version of Record online: 7 MAR 2014 | DOI: 10.1111/tra.12160

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      Mutation of the inositol 5-phophatase OCRL1 causes two disorders in humans, namely Lowe syndrome and Dent-2 disease. Significant progress in understanding the functions of OCRL1 has been made in recent years, indicating a role for the protein in diverse cellular processes. Moreover, the recent emergence of animal models has provided new insights into the mechanisms by which loss of OCRL1 leads to disease. Here, we review recent advances in understanding OCRL1 made at both the cellular and organismal level.

  3. Original Articles

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      Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins (pages 488–499)

      Florian A. Horenkamp, Shaeri Mukherjee, Eric Alix, Curtis M. Schauder, Andree M. Hubber, Craig R. Roy and Karin M. Reinisch

      Version of Record online: 12 MAR 2014 | DOI: 10.1111/tra.12158

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      The bacterial effector protein SidC and its paralog SdcA have been described as tethering factors encoded by the intracellular pathogen Legionella pneumophila. Here, we demonstrate that SidC proteins are important for early events unique to maturation of vacuoles containing Legionella and discover monoubiquitination of Rab1 as a new SidC-dependent activity. The crystal structure of the SidC N-terminus revealed a novel fold comprising three domains (A–C), where domain C plays a critical role in SidC/SdcA-mediated Rab1 ubiquitination.

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      Subcellular Trafficking and Activity of Hyal-1 and Its Processed Forms in Murine Macrophages (pages 500–515)

      Emeline Puissant, Florentine Gilis, Sophie Dogné, Bruno Flamion, Michel Jadot and Marielle Boonen

      Version of Record online: 11 MAR 2014 | DOI: 10.1111/tra.12162

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      The lysosomal residence of Hyal-1 has never been formally established. Present work reports that Hyal-1 is weakly mannose 6-phosphorylated but traffics to lysosomes in murine macrophages via a mannose 6-phosphate-independent secretion/recapture mechanism that involves the mannose receptor. During transport through endosomes, Hyal-1 is matured into a lower molecular mass form that reaches the lysosomes where its activity can only be efficiently detected in native gel zymography, pointing to noncovalent association of Hyal-1 proteolytic fragments or existence of closely linked partners.

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      Escherichia coli Exposure Inhibits Exocytic SNARE-Mediated Membrane Fusion in Mast Cells (pages 516–530)

      Jordan Wesolowski and Fabienne Paumet

      Version of Record online: 7 MAR 2014 | DOI: 10.1111/tra.12159

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      Mast cell degranulation plays a major role in allergic diseases. Here, we report that co-culturing mast cells with E. coli inhibits FcεRI-mediated degranulation by impacting the function of the exocytic SNARE fusion machinery. In particular, E. coli co-culture reduces the IKKβ-dependent phosphorylation of the t-SNARE SNAP23, thus impairing the formation of ternary exocytic SNARE complexes and ultimately mediator release.

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      Regulated Oligomerization Induces Uptake of a Membrane Protein into COPII Vesicles Independent of Its Cytosolic Tail (pages 531–545)

      Sebastian Springer, Per Malkus, Britta Borchert, Ursula Wellbrock, Rainer Duden and Randy Schekman

      Version of Record online: 25 FEB 2014 | DOI: 10.1111/tra.12157

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      In this study, induced oligomerization of a model transmembrane cargo protein stimulates its ER export in vitro independent of known export signals. Sec24-binding motifs in the cytosolic tail of the protein are not required for incorporation into COPII transport vesicles generated in vitro and instead the efficiency of ER exit is strongly dependent on the degree of oligomerization. We propose that oligomerization of this transmembrane protein induces local membrane bending, which in turn promotes COPII vesicle generation.

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      Yeast Endocytic Adaptor AP-2 Binds the Stress Sensor Mid2 and Functions in Polarized Cell Responses (pages 546–557)

      Bernardo Chapa-y-Lazo, Ellen G. Allwood, Iwona I. Smaczynska-de Rooij, Mary L. Snape and Kathryn R. Ayscough

      Version of Record online: 25 FEB 2014 | DOI: 10.1111/tra.12155

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      AP-2 complex in Candida albicans is required for normal hyphal growth. Budding yeast AP-2 has an important function in cell polarity responses to pheromone, nutritional status and cell wall damage. AP-2 binds to the cell wall stress receptor Mid2 and is required for its relocalization in response to pheromone and cell wall damage by calcofluor. AP-2 binds Mid2 at a site which includes a YXXΦ motif but mutation at this site is not sufficient to inhibit Mid2 relocalization.

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      A Dynamin Homolog Promotes the Transition from Hemifusion to Content Mixing in Intracellular Membrane Fusion (pages 558–571)

      Aditya Kulkarni, Kannan Alpadi, Tirupataiah Sirupangi and Christopher Peters

      Version of Record online: 25 FEB 2014 | DOI: 10.1111/tra.12156

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      Dynamin family members have been implicated in exocytosis. Vps1 (the yeast dynamin homolog) mutant vacuoles show decreased fusion and trans-Soluble N-ethylmaleimide sensitive factor Attachment Protein Receptor (SNARE) complex formation but comparable hemifusion relative to wild type. Vps1, through its oligomerization and SNARE-domain binding, brings together multiple t-SNAREs. This finding uncovers a novel function of Vps1 in coordinating the hemifusion – content mixing transition in yeast vacuole fusion.

  4. Toolbox

    1. Top of page
    2. Issue Information
    3. Review
    4. Original Articles
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      High-Throughput Quantitation of Intracellular Trafficking and Organelle Disruption by Flow Cytometry (pages 572–582)

      Pei Zhi Cheryl Chia, Yasmin M. Ramdzan, Fiona J. Houghton, Danny M. Hatters and Paul A. Gleeson

      Version of Record online: 11 MAR 2014 | DOI: 10.1111/tra.12161

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      Standard approaches for analysing the intracellular location of membrane cargo involve microscopy-based methods, which have limitations in throughput capacity and acquisition speed. We describe a flow cytometry-based method, which allows 1000s of cells to be analysed per second. We demonstrate that fluorescence pulse-width, a standard parameter of flow cytometers, can be used to determine the location of membrane proteins, to monitor their trafficking and can be exploited to sort cells based on differences in the intracellular localization of membrane proteins.

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