Cover image for Vol. 17 Issue 6

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


  1. 1 - 14
  1. Original Articles

    1. You have full text access to this OnlineOpen article
      A Genetic Screen Identifies a Critical Role for the WDR81-WDR91 Complex in the Trafficking and Degradation of Tetherin

      Radu Rapiteanu, Luther J. Davis, James C. Williamson, Richard T. Timms, J. Paul Luzio and Paul J. Lehner

      Version of Record online: 25 MAY 2016 | DOI: 10.1111/tra.12409

      Thumbnail image of graphical abstract

      A genetic screen in human haploid cells identifies a critical role for the WDR81-WDR91 complex in the degradation of tetherin – a potent viral restriction factor. Subsequent experiments show that this complex plays a general role in the degradation of internalized plasma membrane proteins as it is also required for EGFR degradation. Depletion of WDR81 leads to the appearance of markedly enlarged early and late endocytic vesicles and to impaired delivery of cargo to lysosomes.

  2. Reviews

    1. Herpesvirus Entry into Host Cells Mediated by Endosomal Low pH

      Anthony V. Nicola

      Version of Record online: 24 MAY 2016 | DOI: 10.1111/tra.12408

      Thumbnail image of graphical abstract

      Herpesviridae comprise a large family of enveloped DNA viruses that utilize several cellular entry pathways in a cell-type-dependent manner. This review focuses primarily on our understanding of low pH entry mechanisms, with emphasis on the prototype alphaherpesvirus, herpes simplex virus 1 (HSV-1). In our model of infection, HSV-1 enters epithelial cells by a mildly acidic endosomal pathway, and HSV-1 entry into neurons, the site of latency, occurs by direct penetration at the cell surface. Low pH-triggered conformational changes in envelope glycoproteins, particularly the main fusion protein gB, are also described.

  3. Traffic Interchanges

    1. Editorial Overview: Myosins in Review

      John Kendrick-Jones and Folma Buss

      Version of Record online: 24 MAY 2016 | DOI: 10.1111/tra.12405

  4. Reviews

    1. Cadherin Trafficking for Tissue Morphogenesis: Control and Consequences

      Junior J. West and Tony J. C. Harris

      Version of Record online: 19 MAY 2016 | DOI: 10.1111/tra.12407

      Thumbnail image of graphical abstract

      Tissue morphogenesis often requires the redistribution of cadherin cell–cell adhesion molecules through trafficking. We review the upstream control and downstream consequences of this trafficking in a variety of model systems. We describe how core trafficking machinery integrates with other molecular systems to control cadherin endocytosis, exocytosis and recycling, and how this trafficking has permissive and instructive effects on various aspects of multicellular development.

  5. Original Articles

    1. Monomerization and ER Relocalization of GRASP Is a Requisite for Unconventional Secretion of CFTR

      Jiyoon Kim, Shin Hye Noh, He Piao, Dong Hee Kim, Kuglae Kim, Jeong Seok Cha, Woo Young Chung, Hyun-Soo Cho, Joo Young Kim and Min Goo Lee

      Version of Record online: 18 MAY 2016 | DOI: 10.1111/tra.12403

      Thumbnail image of graphical abstract

      Endoplasmic reticulum (ER)-to-Golgi blockade or ER stress induces Golgi reassembly stacking protein (GRASP)-mediated, Golgi-bypassing cell-surface trafficking of the folding-deficient ΔF508-cystic fibrosis transmembrane conductance regulator (CFTR). Here, we show the mechanism by which the Golgi protein GRASP accesses the ER-retained ΔF508-CFTR, which may offer insights toward therapeutic strategies for cystic fibrosis. ER stress-associated signals induce phosphorylation-dependent dissociation of GRASP55 complexes and significant amounts of disassembled GRASP55 undergo relocalization into the ER. Migration of GRASP55 to the ER enables the association with ΔF508-CFTR via a PSD95/Dlg1/ZO-1-based interaction and subsequent unconventional surface trafficking of CFTR.

  6. Reviews

    1. Multiple Roles of VARP in Endosomal Trafficking: Rabs, Retromer Components and R-SNARE VAMP7 Meet on VARP

      Mitsunori Fukuda

      Version of Record online: 13 MAY 2016 | DOI: 10.1111/tra.12406

      Thumbnail image of graphical abstract

      VARP/ANKRD27 was originally identified as a VPS9-domain-containing protein that possesses guanine nucleotide exchange factor activity toward small GTPase Rab21. A number of VARP-interacting molecules have recently been identified, and VARP is now known to interact with three different types of key membrane trafficking regulators, i.e. small GTPase Rabs (Rab32, Rab38 and Rab40C), retromer components (VPS29 and VSP35) and R-SNARE VAMP7. By binding to several of these molecules, VARP plays pivotal roles in endosomal trafficking, which underlies a variety of cellular events.

  7. Original Articles

    1. Ligation of FcγR Alters Phagosomal Processing of Protein via Augmentation of NADPH Oxidase Activity

      Dale R. Balce, Joanna M. Rybicka, Catherine J. Greene, Benjamin W. Ewanchuk and Robin M. Yates

      Version of Record online: 13 MAY 2016 | DOI: 10.1111/tra.12396

      Thumbnail image of graphical abstract

      Protein degradation is influenced by redox conditions in the phagosome. Here we show that differential NADPH oxidase (NOX2) activation, as a consequence of Fcγ-receptor ligation, results in phagosome-specific changes in redox-sensitive protein processing. Phagosomes that contained opsonized cargo generated high levels of reactive oxygen species (ROS) which subsequently decreased the rates of reduction and hydrolysis of phagocytosed protein. This occurred in an autonomous fashion. These findings indicate that opsonized proteins are differentially degraded within phagosomes via redox control of phagosomal function.

    2. Creating a chimeric clathrin heavy chain that functions independently of yeast clathrin light chain

      Douglas R. Boettner, Verónica A. Segarra, Balaji T. Moorthy, Nagore de León, John Creagh, John R. Collette, Arun Malhotra and Sandra K. Lemmon

      Version of Record online: 11 MAY 2016 | DOI: 10.1111/tra.12401

    3. Human Fumarate Hydratase Is Dual Localized by an Alternative Transcription Initiation Mechanism

      Ekaterina Dik, Adi Naamati, Hadar Asraf, Norbert Lehming and Ophry Pines

      Version of Record online: 6 MAY 2016 | DOI: 10.1111/tra.12397

      Thumbnail image of graphical abstract

      Schematic model of human FH (fumarate hydratase) distribution mechanism. A) FH is transcribed from a single gene harboring a broad type promoter. Transcription starts from various transcription start sites (TSS), creating different length mRNAs. B) All mRNAs harboring a sequence longer than 15 nt upstream of the first AUG, will be translated from the first AUG (left, orange arrow). These will give rise to the MTS (mitochondrial targeting sequence) harboring FH which will be directed to the mitochondria. C) mRNAs which are transcribed closer to the first ATG or after, will be translated from the second AUG (right, blue arrow).

  8. Reviews

    1. Tropomyosin-Mediated Regulation of Cytoplasmic Myosins

      Dietmar J. Manstein and Daniel P. Mulvihill

      Version of Record online: 4 MAY 2016 | DOI: 10.1111/tra.12399

      Thumbnail image of graphical abstract

      The metazoan actin-based cytoskeleton facilitates an assortment of diverse cellular functions. This is made possible by the members of the tropomyosin multigene family, which at discrete cellular locations form well-defined copolymers with unique functional properties. Here, we present a unifying theory in which the tropomyosin isoform associating with the actin defines the surface landscape of the copolymer to determine the identity and activity of myosin motors that move upon it.

  9. Transit Authority

    1. Use of a Grant Writing Class in Training PhD Students

      Richard A. Kahn, Graeme L. Conn, Grace K. Pavlath and Anita H. Corbett

      Version of Record online: 3 MAY 2016 | DOI: 10.1111/tra.12398

  10. Reviews

    1. Mechanics and Activation of Unconventional Myosins

      Christopher Batters and Claudia Veigel

      Version of Record online: 3 MAY 2016 | DOI: 10.1111/tra.12400

      Thumbnail image of graphical abstract

      A model showing an idealized unconventional myosin summarizing some of the mechanical specializations that they possess including the ability to backfold and unfold in the presence of calcium; for calmodulin to bind, rebind and change conformation; to produce the working stroke in two phases; to be dimeric and processive; to sense strain and to alter the kinetics dependent on the external load. The motor domains are shown in blue, the calmodulin/light chains are in yellow.

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

      Jianchao Li, Qing Lu and Mingjie Zhang

      Version of Record 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.


  1. 1 - 14