Cover image for Vol. 17 Issue 5

Early View (Online Version of Record published before inclusion in an issue)

Edited By: Michael S. Marks, Trina A. Schroer, Tom H. Stevens and Sharon A. Tooze

Online ISSN: 1600-0854


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  1. Original Articles

    1. Lipid Droplets Form from Distinct Regions of the Cell in the Fission Yeast Schizosaccharomyces pombe

      Alex Meyers, Zuania P. del Rio, Rachael A. Beaver, Ryan M. Morris, Taylor M. Weiskittel, Amany K. Alshibli, Jaana Mannik, Jennifer Morrell-Falvey and Paul Dalhaimer

      Article first published online: 29 APR 2016 | DOI: 10.1111/tra.12394

      Thumbnail image of graphical abstract

      The authors show that lipid droplets form from different regions of fission yeast Schizosaccharomyces pombe cells based on the dominant neutral lipid of the nascent droplet. Droplets that are enriched in sterol esters form at the tips of polarized cells, whereas droplets that are enriched in triacylglycerols (TAGs) form around the nucleus. Elimination of TAGs completely abolishes lipid droplets, instead vesicle-shaped BODIPY 493/503 structures are observed. Thus, TAG seems necessary for lipid droplet biogenesis in these yeast cells.

  2. Reviews

    1. You have free access to this content
      Co- and Post-Translational Protein Folding in the ER

      Lars Ellgaard, Nicholas McCaul, Anna Chatsisvili and Ineke Braakman

      Article first published online: 22 APR 2016 | DOI: 10.1111/tra.12392

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      The endoplasmic reticulum (ER) produces a plethora of membrane and secretory proteins, which must fold and assemble correctly before ER exit – if these processes fail, misfolded species accumulate in the ER or are degraded. Here, we review chaperone-assisted co- and post-translational folding and assembly in the ER and the influence of protein modifications, emphasizing how method development has advanced the field by allowing folding studies inside living cells. The laboratory of Dr Ari Helenius pioneered many of these studies with the influenza virus hemagglutinin (HA) protein, which is a trimer. This cartoon of an HA monomer drawn by Dr Ari Helenius shows the receptor domain (R), the esterase-like domain (E′) and the stem domain (S). Native HA has six disulfide bonds (orange lines). A, B, E, F1 and F2 indicate the positions of antigenic epitopes.

  3. Original Articles

    1. You have free access to this content
      Differential Use of the C-Type Lectins L-SIGN and DC-SIGN for Phlebovirus Endocytosis

      Psylvia Léger, Marilou Tetard, Berthe Youness, Nicole Cordes, Ronan N. Rouxel, Marie Flamand and Pierre-Yves Lozach

      Article first published online: 21 APR 2016 | DOI: 10.1111/tra.12393

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      The receptors and cellular factors used by phleboviruses (Bunyaviridae) to enter host cells remain largely unidentified. In addition to the C-type lectin DC-SIGN (Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin), we report here that several phleboviruses subvert the closely related protein L-SIGN for infection. Together, our results establish that L-SIGN is an attachment factor not required for virus internalization whereas DC-SIGN is an authentic entry receptor required for both binding and endocytosis. Our study underlines the importance of the subsequent entry processes in virus–receptor interactions beyond attachment.

  4. Reviews

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      Fusion of Enveloped Viruses in Endosomes

      Judith M. White and Gary R. Whittaker

      Article first published online: 7 APR 2016 | DOI: 10.1111/tra.12389

      Thumbnail image of graphical abstract

      To initiate infection, enveloped viruses must fuse with a cell membrane, a process mediated by a dedicated viral fusion protein. To date, these proteins group into three basic structural classes. Most require priming (via a protease) to prepare them to respond to a fusion-triggering signal. Known fusion triggers include receptors, low pH and proteases (and combinations thereof). Here, we provide an update on viral fusion protein priming and triggering, with a focus on virus fusion in endosomes.

  5. Original Articles

    1. Regulation of Cell Migration and β1 Integrin Trafficking by the Endosomal Adaptor GGA3

      Colin D. H. Ratcliffe, Pranshu Sahgal, Christine A. Parachoniak, Johanna Ivaska and Morag Park

      Article first published online: 5 APR 2016 | DOI: 10.1111/tra.12390

      Thumbnail image of graphical abstract

      Upon internalization, integrin receptors may enter an endosomal recycling pathway or be targeted for degradation via the late endosome/lysosome. Recycling of integrins to restricted subcellular domains is required for efficient cell migration. The Golgi-localized gamma ear-containing Arf-binding (GGA) family of proteins (GGA1, GGA2 and GGA3) are adaptor proteins that promote clathrin assembly and mediate intracellular transport of receptors. Here we identify a role for GGA3 in regulating cell migration, focal adhesions and trafficking of β1 integrin.

  6. Toolbox

    1. A Toolbox for Rapid Quantitative Assessment of Chronological Lifespan and Survival in Saccharomyces cerevisiae

      Sarah R. Chadwick, Athanasios D. Pananos, Sonja E. Di Gregorio, Anna E. Park, Parnian Etedali-Zadeh, Martin L. Duennwald and Patrick Lajoie

      Article first published online: 1 APR 2016 | DOI: 10.1111/tra.12391

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      The yeast Saccharomyces cerevisiae provides an unmatched genetic platform to study the mechanisms underlying the aging process. We present a rapid and efficient quantitative assay to measure chronological aging in yeast through fluorescent labeling of dead cells in multiwell plates. We designed an open-source software to rapidly quantify yeast survival under various conditions, including chronological aging. We employed our assays to study the role of different heat shock proteins in the extension of yeast chronological lifespan by caloric restriction.

  7. Reviews

    1. You have free access to this content
      Principles of Virus Uncoating: Cues and the Snooker Ball

      Yohei Yamauchi and Urs F. Greber

      Article first published online: 31 MAR 2016 | DOI: 10.1111/tra.12387

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      The architecture of a virus particle allows timely release of the viral genome in a host cell during entry. This critical step is known as viral uncoating. It is regulated by cues from receptors, enzymes and chemicals, and facilitated by factors that do not contact the virion directly. This review covers a wide range of cellular processes that enhance viral uncoating. The underlying mechanisms provide deep insights into cell biological and immunological processes of virus–host interactions and infections.

    2. Structural Basis of Cargo Recognition by Unconventional Myosins in Cellular Trafficking

      Jianchao Li, Qing Lu and Mingjie Zhang

      Article first published online: 17 MAR 2016 | DOI: 10.1111/tra.12383

      Thumbnail image of graphical abstract

      Unconventional myosins play critical roles in many aspects of cellular tracking processes via binding to different cargo proteins as well as lipid vesicles. This review focuses on the structural basis of cargo recognitions and cargo binding-induced motor activity regulations of several unconventional myosins with prominent roles in cellular trafficking.


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