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Cover image for Vol. 15 Issue 1

January 2014

Volume 15, Issue 1

Pages i–i, 1–126

  1. Issue Information

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      Issue Information (page i)

      Version of Record online: 6 DEC 2013 | DOI: 10.1111/tra.12103

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      Simple and Direct Assembly of Kymographs from Movies Using KYMOMAKER (pages 1–11)

      Kyoko Chiba, Yuki Shimada, Masataka Kinjo, Toshiharu Suzuki and Seiich Uchida

      Version of Record online: 31 OCT 2013 | DOI: 10.1111/tra.12127

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      KYMOMAKER is an open access program that allows cell biologists to easily and directly generate kymographs from movies. This software can automatically extract faint traces; therefore, it is particularly useful for analyzing low levels of fluorescently labeled vesicular cargos in axons. Filters can be applied to remove Brownian motion. Color kymographs can be generated that include the position of the cargo perpendicular to the long axis of the axon, information that is lost in traditional kymographs.

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      Dissecting Functions of the Conserved Oligomeric Golgi Tethering Complex Using a Cell-Free Assay (pages 12–21)

      Nathanael P. Cottam, Katherine M. Wilson, Bobby G. Ng, Christian Körner, Hudson H. Freeze and Daniel Ungar

      Version of Record online: 31 OCT 2013 | DOI: 10.1111/tra.12128

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      Intra-Golgi vesicle transport was reconstituted in vitro using fluorescently marked galactosyltransferase as a marker. Microscopic analysis of transport reactions provides the readout, and shows physiological properties of the reconstitution, including protein, energy and temperature dependence. The new assay was used to show antagonistic functions of the two halves of the conserved oligomeric Golgi complex during trans-Golgi vesicle tethering. The assay will be particularly useful to study molecular determinants of tethering, and human congenital glycosylation disorders that affect Golgi trafficking.

  3. Case Report

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      Microvillus Inclusion Disease: Loss of Myosin Vb Disrupts Intracellular Traffic and Cell Polarity (pages 22–42)

      Cornelia E. Thoeni, Georg F. Vogel, Ivan Tancevski, Stephan Geley, Silvia Lechner, Kristian Pfaller, Michael W. Hess, Thomas Müller, Andreas R. Janecke, Yaron Avitzur, Aleixo Muise, Ernest Cutz and Lukas A. Huber

      Version of Record online: 19 NOV 2013 | DOI: 10.1111/tra.12131

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      Missense and nonsense mutations in the MYO5B gene cause microvillus inclusion disease (MVID), a congenital enteropathy characterized by loss of apical microvilli and cytoplasmic microvillus inclusions. A non-functional myosin Vb motor in mature enterocytes results in disorganized actin filaments, interruption of intracellular vesicle trafficking manifesting by redistributed Rab GTPases (Rab11, Rab9 and Rab8), mislocalized cell organelle markers (EEA1 and LAMP2) and transporter proteins (CD36, TfR and Na/K ATPase). This results in impaired intestinal barrier formation and severe loss of epithelial polarity.

  4. Original Articles

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      Targeted Disruption of an EH-domain Protein Endocytic Complex, Pan1-End3 (pages 43–59)

      Karen Whitworth, Mary Katherine Bradford, Nicole Camara and Beverly Wendland

      Version of Record online: 31 OCT 2013 | DOI: 10.1111/tra.12125

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      Pan1 is an endocytic scaffold that interacts with structural and regulatory endocytic components. Pan1 is composed of Eps15 Homology (EH) domains that bind adaptor proteins, a central oligomerization domain and C-terminal binding sites for Arp2/3, F-actin and type-I myosin motors. We show that the central domain of Pan1 binds its constitutive partner End3, another EH domain protein, via the two C-terminal End3 Repeats (which are absent in end3-1). The conserved hydrophilic faces of the End3 Repeats mediate Pan1 binding.

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      Disruption of Clathrin-Mediated Trafficking Causes Centrosome Overduplication and Senescence (pages 60–77)

      Maciej B. Olszewski, Panagiotis Chandris, Bum-Chan Park, Evan Eisenberg and Lois E. Greene

      Version of Record online: 12 NOV 2013 | DOI: 10.1111/tra.12132

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      Knocking out GAK, a HSC70 cochaperone essential for chaperoning clathrin causes senescence and centrosome overduplication. Disruption of clathrin-mediated endocytosis leads to alterations in mitogenic signaling profile which causes growth arrest and centrosome overduplication. Concurrent disruption of intracellular clathrin-dependent trafficking results in lysosomal membrane destabilization causing iron leakage that leads to DNA damage. Prolonged exposure to DNA damage in the presence of mitogenic stimulation leads to the development of senescence accompanied by centrosome overduplication.

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      The Fate of PrP GPI-Anchor Signal Peptide is Modulated by P238S Pathogenic Mutation (pages 78–93)

      Gianni Guizzunti and Chiara Zurzolo

      Version of Record online: 31 OCT 2013 | DOI: 10.1111/tra.12126

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      The fate of GPI-anchor signal peptides (GPI-SPs) is currently unknown. PrP GPI-SP shows a remarkable and unusual level of conservation across species and contains two point mutations responsible for genetic cases of prion diseases. Here we show that differently from folate receptor, PrP GPI-SP is specifically degraded via the proteasome. Furthermore the P238S pathogenic mutation protects the peptide from degradation, leading to its endoplasmic reticulum accumulation. This opens the possibility that PrP GPI-SP plays a role in neurodegenerative prion diseases.

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      PEX5, the Shuttling Import Receptor for Peroxisomal Matrix Proteins, Is a Redox-Sensitive Protein (pages 94–103)

      Oksana Apanasets, Cláudia P. Grou, Paul P. Van Veldhoven, Chantal Brees, Bo Wang, Marcus Nordgren, Gabriele Dodt, Jorge E. Azevedo and Marc Fransen

      Version of Record online: 31 OCT 2013 | DOI: 10.1111/tra.12129

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      Mounting evidence suggests that oxidative stress impairs peroxisomal matrix protein import. This study provides direct evidence that the import of PTS1 matrix proteins into peroxisomes is indeed a redox-regulated process, and that this redox-sensitivity is mediated by PEX5, the shuttling receptor for PTS1 proteins. In addition, it demonstrates that Cys11 of human PEX5 functions as a redox switch that modulates PEX5 activity in response to intracellular oxidative stress, most likely by modulating its monoubiquitination at the peroxisomal membrane.

  5. Traffic Interchanges

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      Longin and GAF Domains: Structural Evolution and Adaptation to the Subcellular Trafficking Machinery (pages 104–121)

      Nicola De Franceschi, Klemens Wild, Alexander Schlacht, Joel B. Dacks, Irmgard Sinning and Francesco Filippini

      Version of Record online: 11 NOV 2013 | DOI: 10.1111/tra.12124

      Longin domains were likely to be present in the Last Eukaryotic Common Ancestor as ‘building blocks’ of the trafficking machinery. The unique fold topology of the seven conserved Longin superfamilies possibly accounts for their special adaptation to – and proliferation within – the eukaryotic trafficking machinery. Comparative analysis of Longin and GAF domains reveals three binding regions (A, B and C) mediating: A, intra- and inter-molecular interactions; B, binding to small GTPases and C, integration into the endomembrane trafficking complexes.

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      Have We Neglected the Role of Fetal Endothelium in Transplacental Transport? (pages 122–126)

      David Elad, Riki Levkovitz, Ariel J. Jaffa, Gernot Desoye and Moshe Hod

      Version of Record online: 8 NOV 2013 | DOI: 10.1111/tra.12130

      In human maternal-to-fetal transplacental transport of substances occurs across syncytiotrophoblast (STB) on the maternal side and endothelial cells (EC) on the fetal side. Numerous studies explored the transport characteristics across the STB layer with very little attention to EC. Recently, a new experimental model revealed significant resistance of the EC layer for transfer of glucose and marker molecules. Hence, it is recommended to direct future research efforts on the relative role of the feto-placental endothelium in contributing to transplacental transport characteristics.

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