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Cover image for Vol. 14 Issue 12

December 2013

Volume 14, Issue 12

Pages 1193–1301

  1. Editorial

    1. Top of page
    2. Editorial
    3. Review
    4. Toolbox
    5. Original Articles
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      Trafficking to a Nobel Prize (page 1193)

      Mark Marsh, Michael Marks, Trina Schroer and Tom Stevens

      Article first published online: 11 NOV 2013 | DOI: 10.1111/tra.12133

  2. Review

    1. Top of page
    2. Editorial
    3. Review
    4. Toolbox
    5. Original Articles
    1. You have full text access to this OnlineOpen article
      Dynamin Rings: Not Just for Fission (pages 1194–1199)

      Sanja Sever, Joann Chang and Changkyu Gu

      Article first published online: 19 SEP 2013 | DOI: 10.1111/tra.12116

      Thumbnail image of graphical abstract

      Dynamin is essential for regulation of actin cytoskeleton, though its mode of action is currently unknown. Recently, direct dynamin–actin interactions and actin-dependent dynamin oligomerization have been identified. Actin-dependent dynamin oligomerization has been linked to formation of free barbed ends, and thus actin polymerization in vitro. Here we discuss the possibility that actin-dependent dynamin oligomerization plays a major role in regulating the actin cytoskeleton via its effect on actin polymerization at distinct sites in the cell.

  3. Toolbox

    1. Top of page
    2. Editorial
    3. Review
    4. Toolbox
    5. Original Articles
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      Automated Quantification of the Subcellular Localization of Multicompartment Proteins via Q-SCAn (pages 1200–1208)

      Nicholas C. Bauer, Anita H. Corbett and Paul W. Doetsch

      Article first published online: 10 OCT 2013 | DOI: 10.1111/tra.12118

      Thumbnail image of graphical abstract

      In eukaryotic cells, proteins can occupy multiple intracellular compartments and move between compartments to fulfill critical biological functions. Unfortunately, no methods have been developed to robustly measure the distribution of a protein among compartments. To address this need, we have developed an automated method termed quantitative subcellular compartmentalization analysis (Q-SCAn). Q-SCAn is a quantitative analytical tool for providing broader and more detailed analysis of the localization of multicompartment proteins as compared to the currently available approaches.

  4. Original Articles

    1. Top of page
    2. Editorial
    3. Review
    4. Toolbox
    5. Original Articles
    1. You have free access to this content
      Golgi-mediated Glycosylation Determines Residency of the T2 RNase Rny1p in Saccharomyces cerevisiae (pages 1209–1227)

      Natalia Shcherbik

      Article first published online: 10 OCT 2013 | DOI: 10.1111/tra.12122

      Thumbnail image of graphical abstract

      The molecular mechanisms controlling intra- and extracellular localization of secretory RNases from the T2 family are unknown. In this study, we found that the T2 RNase Rny1p from budding yeast undergoes glycosylation in the ER, followed by glycosylation inside the Golgi compartment. The latter modification is necessary for the extracellular secretion of Rny1p. Golgi-glycosylation deficient nuclease remains inside the cell, and can translocate to the vacuole. Our results demonstrate the role of Golgi-mediated glycosylation in T2 RNase traffic and secretion.

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      Saturated Fatty Acids Alter the Late Secretory Pathway by Modulating Membrane Properties (pages 1228–1241)

      Laurie-Anne Payet, Ludovic Pineau, Ellen C. R. Snyder, Jenny Colas, Ahmed Moussa, Brigitte Vannier, Joelle Bigay, Jonathan Clarhaut, Frédéric Becq, Jean-Marc Berjeaud, Clarisse Vandebrouck and Thierry Ferreira

      Article first published online: 2 OCT 2013 | DOI: 10.1111/tra.12117

      Thumbnail image of graphical abstract

      Excess palmitate can be driven to the phospholipid (PL) pathway, leading to high saturated PL-levels. We show here that saturated PL reduce the number of secretory vesicles ‘en route’ to the plasma membrane. On a mechanistic point of view, SFA accumulation within PL shifts PL shape from conical to cylindrical. This results in an increase in lipid packing which, in turn, alters the recruitment of loose lipid packing-sensing proteins (e.g. Gcs1p), required for optimal budding, to nascent vesicles.

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      RhoD Binds the Rab5 Effector Rabankyrin-5 and has a Role in Trafficking of the Platelet-derived Growth Factor Receptor (pages 1242–1254)

      Vishal Nehru, Oleksandr Voytyuk, Johan Lennartsson and Pontus Aspenström

      Article first published online: 10 OCT 2013 | DOI: 10.1111/tra.12121

      Thumbnail image of graphical abstract

      We discovered that RhoD binds to the Rab5 effector Rabankyrin-5, and RhoD and Rabankyrin-5 colocalize to Rab5-positive endosomes, which suggests a role for Rabankyrin-5 in the coordination of RhoD and Rab5 in endosomal trafficking. Depletion of RhoD using siRNA techniques interfered with the internalization of the PDGF β receptor and the subsequent activation of the downstream signaling cascades. Our data implicate that RhoD and Rabankyrin-5 have important roles in coordinating RhoD and Rab activities during trafficking of the PDGF β receptor.

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      EphA2 Signaling Following Endocytosis: Role of Tiam1 (pages 1255–1271)

      Pomme Boissier, Jin Chen and Uyen Huynh-Do

      Article first published online: 10 OCT 2013 | DOI: 10.1111/tra.12123

      Thumbnail image of graphical abstract

      Eph receptors, a complex subfamily of receptor tyrosine kinases, are rapidly endocytosed following ligand-mediated activation and traffic through endocytic compartments prior to degradation. Here, we depict the trafficking of the angiogenic and tumorigenic EphA2 receptors and show that a part of them are recycled back to the plasma membrane. Our study also demonstrates for the first time that EphA2 retains the capacity to signal in endosomes. In particular, our findings establish Tiam1, a Rac1-specific GEF, as an important modulator of EphA2 signaling.

    5. You have full text access to this OnlineOpen article
      Building a Better Dynasore: The Dyngo Compounds Potently Inhibit Dynamin and Endocytosis (pages 1272–1289)

      Adam McCluskey, James A. Daniel, Gordana Hadzic, Ngoc Chau, Emma L. Clayton, Anna Mariana, Ainslie Whiting, Nick N. Gorgani, Jonathan Lloyd, Annie Quan, Lia Moshkanbaryans, Sai Krishnan, Swetha Perera, Megan Chircop, Lisa von Kleist, Andrew B. McGeachie, Mark T. Howes, Robert G. Parton, Michael Campbell, Jennette A. Sakoff, Xuefeng Wang, Jian-Yuan Sun, Mark J. Robertson, Fiona M. Deane, Tam H. Nguyen, Frederic A. Meunier, Michael A. Cousin and Phillip J. Robinson

      Article first published online: 9 OCT 2013 | DOI: 10.1111/tra.12119

      Thumbnail image of graphical abstract

      Dynamin is essential for clathrin-mediated endocytosis (CME). We describe the Dyngo™ series of dynamin inhibitors with greatly improved potency, reduced cytotoxicity and reduced detergent binding compared to their parent, dynasore. Dyngo compound 4a is 37-fold more potent for dynamin inhibition and at least sixfold more potent for CME inhibition in cells and nerve terminals. This series are the first to target one conformational state of dynamin, inhibiting lipid-associated helical dynamin but not dynamin rings induced by self-assembly or SH3-domain-containing proteins.

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      Distinct Ubiquitination Cascades Act on the Peroxisomal Targeting Signal Type 2 Co-receptor Pex18p (pages 1290–1301)

      Fouzi El Magraoui, Rebecca Brinkmeier, Andreas Schrötter, Wolfgang Girzalsky, Thorsten Müller, Katrin Marcus, Helmut E. Meyer, Ralf Erdmann and Harald W. Platta

      Article first published online: 7 OCT 2013 | DOI: 10.1111/tra.12120

      Thumbnail image of graphical abstract

      The peroxisomal targeting signal type 2 co-receptor Pex18p is polyubiquitinated on lysine residues and monoubiquitinated on a conserved cysteine. In this study, we have identified the two corresponding ubiquitination cascades that catalyze these modifications. We demonstrate that polyubiquitination of Pex18p requires the ubiquitin-conjugating enzyme (E2) Ubc4p, which cooperates with the RING (really interesting new gene)-type ubiquitin-protein ligases (E3) Pex2p as well as Pex10p. Monoubiquitination of Pex18p is catalyzed by the E2 enzyme Pex4p which acts in concert with the E3 enzymes Pex12p and Pex10p.

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