Cover image for Vol. 17 Issue 2

Accepted Articles (Accepted, unedited articles published online and citable. The final edited and typeset version of record will appear in future.)

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

Online ISSN: 1600-0854


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  1. Transit Authority

    1. My early days with Ari Helenius: detergents and viruses

      Kai Simons

      Accepted manuscript online: 12 FEB 2016 08:07AM EST | DOI: 10.1111/tra.12377

  2. Original Articles

    1. A Systematic Cell-Based Analysis of Localization of Predicted Drosophila Peroxisomal Proteins

      Matthew N. Baron, Christen M. Klinger, Richard A. Rachubinski and Andrew J. Simmonds

      Accepted manuscript online: 11 FEB 2016 12:45AM EST | DOI: 10.1111/tra.12384

      Thumbnail image of graphical abstract

      Peroxisome biogenesis in Drosophila peroxisomes. Drosophila peroxisomes consist of a membrane (black) surrounding a protein matrix (blue). In peroxisome targeting sequence 1 (PTS1) directed matrix protein import (red), Pex5 (5) binds PTS1 and traffics its cargo to the peroxisomal membrane, where it interacts with the pore-forming complex comprised of Pex13 (13) and Pex14 (14) and the RING-finger complex made up of Pex2 (2), Pex10 (10) and Pex12 (12). Pex5 and its cargo cross the peroxisomal membrane, and Pex5 dissociates from its cargo in the peroxisomal matrix and is recycled to the cytosol by a complex composed of the AAA-ATPases Pex1 and Pex6, an unknown membrane anchor (X), and the RING-finger complex (green). Other matrix proteins lacking a canonical PTS1 are trafficked to the peroxisome by an unknown factor (black, X). There is no evidence of a PTS2 import pathway in Drosophila. A protein (7?) homologous to the PTS2 receptor Pex7 of other organisms localizes to both the cytosol and the peroxisome; its function is undetermined. In peroxisomal membrane protein targeting (mPTS, purple), Pex19 binds to a mPTS and traffics cargo to the peroxisome, where it interacts with Pex3 (3) in complex with Pex16 (16). The mPTS-containing cargo is inserted into the peroxisomal membrane, and Pex19 (19) is released back to the cytosol. Peroxisomal membrane protein targeting can also occur at the level of the endoplasmic reticulum (not shown). Mature peroxisomes can proliferate by fission (orange), in which Pex11A/B (11A/B) and Pex11C (11C) participate in the elongation of the peroxisome and its scission into two daughter organelles.

    2. Dynamin-actin cross-talk contributes to phagosome formation and closure

      Florence Marie-Anaïs, Julie Mazzolini, Floriane Herit and Florence Niedergang

      Accepted manuscript online: 5 FEB 2016 01:15AM EST | DOI: 10.1111/tra.12386

      Thumbnail image of graphical abstract

      Phagosome formation relies on profound reorganization of actin and membranes, but the mechanism of phagosome closure remains poorly understood. We used an original experimental set up to monitor phagosome formation and closure in three dimensions in living macrophages using Total Internal Reflection Fluorescence (TIRF) Microscopy. We reveal that a crosstalk between actin and dynamin-2 takes place for phagosome formation and closure, and that dynamin-2 plays a critical role in the effective scission of phagosomes from the plasma membrane.

    3. Engineered tug-of-war between kinesin and dynein controls direction of microtubule transport in vivo

      Karim Rezaul, Dipika Gupta, Irina Semenova, Kazuho Ikeda, Pavel Kraikivski, Ji Yu, Ann Cowan, Ilya Zaliapin and Vladimir Rodionov

      Accepted manuscript online: 4 FEB 2016 02:47AM EST | DOI: 10.1111/tra.12385

      Thumbnail image of graphical abstract

      Recruitment of external plus-end directed microtubule motor kinesin-1 to the surface of pigment granules transported to microtubule minus-ends by cytoplasmic dynein in melanophores creates a tug-of-war between opposing microtubule motors in vivo. Loading with kinesin-1 attenuates minus-end directed runs of pigment granules generated by dynein, and reverses the overall direction of their movement. Therefore in the absence of external signals, a tug-of-war between opposing microtubule motors is sufficient to control the directionality of microtubule transport in vivo.

  3. Reviews

    1. Space: a final frontier for vacuolar pathogens

      Elizabeth Di Russo Case, Judith A. Smith, Thomas A. Ficht, James E. Samuel and Paul de Figueiredo

      Accepted manuscript online: 4 FEB 2016 02:16AM EST | DOI: 10.1111/tra.12382

      Thumbnail image of graphical abstract

      Intracellular bacteria must appropriate host vesicular traffic and membrane fusion events to build pathogen-specific niches. Here, we review the molecular mechanisms and trafficking pathways that drive two space allocation strategies of intracellular bacteria, the formation of tight and spacious pathogen-containing vacuoles. We relate bacterial modulation of vacuolar space to its impact on critical facets of intracellular parasitism and discuss the evolutionary drivers that may have shaped their replicative vacuoles.

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

      Jianchao Li, Qing Lu and Mingjie Zhang

      Accepted manuscript online: 4 FEB 2016 02:13AM EST | 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.

  4. Toolbox

    1. Measuring Exocytosis Rate Using Corrected Fluorescence Recovery After Photoconversion

      Nan Luo, An Yan and Zhenbiao Yang

      Accepted manuscript online: 29 JAN 2016 04:38AM EST | DOI: 10.1111/tra.12380

      An optical method is developed to measure the exocytosis rate of plasma membrane or extracellular matrix proteins. In this method, the protein-of-interest is tagged with a green-to-red photoconvertible fluorescent protein; after photoconverting a region-of-interest on the cell surface, exocytosis-dependent and independent trafficking events are tracked simultaneously for accurate determination of exocytosis rate.

  5. Original Articles

    1. A C. elegans homologue of LYST functions in endosome and lysosome-related organelle biogenesis

      Alec Barrett and Greg J. Hermann

      Accepted manuscript online: 29 JAN 2016 04:38AM EST | DOI: 10.1111/tra.12381

      LYST-1 is a C. elegans BEACH domain containing protein (BDCP) homologous to LYST and NBEAL2, BDCPs controlling organelle biogenesis that are implicated in human disease. Unlike the 3 other BDCPs encoded by C. elegans, mutations in lyst-1 lead to smaller lysosome-related organelles (LROs), smaller lysosomes, increased numbers of LROs, and decreased numbers of early endosomes. lyst-1(−) mutations do not obviously disrupt protein trafficking to lysosomes or LROs, however the formation of gut granules is diminished.

    2. Sorting Nexin 11 Regulates Lysosomal Degradation of Plasma Membrane TRPV3

      Caiyue Li, Wenbo Ma, Shikui Yin, Xin Liang, Xiaodong Shu, Duanqing Pei, Terrance M Egan, Jufang Huang, Aihua Pan and Zhiyuan Li

      Accepted manuscript online: 27 JAN 2016 10:06PM EST | DOI: 10.1111/tra.12379

      The trafficking of ion channels to/from the plasma membrane is essential for the functionality of cells. We report the novel finding that the vesicular trafficking protein SNX11 promotes the trafficking of exogenous TRPV3 ion channel from the plasma membrane to lysosome for degradation via protein-protein interactions in HEK293T cells, and it also decreases the level of endogenous TRPV3 protein in human skin keratinocytes HaCaT cells, which leads to a change in the density of TRPV3 channels on the cell surface.

  6. Reviews

    1. Viral genome tethering to host cell chromatin: cause and consequences

      Inci Aydin and Mario Schelhaas

      Accepted manuscript online: 20 JAN 2016 02:26AM EST | DOI: 10.1111/tra.12378

      Thumbnail image of graphical abstract

      Several persisting DNA viruses tether their genomes to mitotic host cell chromatin during cell division. This way, they maintain the viral genomes during cell division of infected cells. Alternatively, they use this feature for nuclear import by exploiting a phase in the cell cycle when the nuclear envelope is disassembled. Tethering may induce severe cellular consequences that involve activation of mitotic checkpoints, missegregation of host chromosomes and genomic instability.

  7. Original Articles

    1. Assembly of peroxisomal membrane proteins via the direct Pex19p-Pex3p pathway

      Yuqiong Liu, Yuichi Yagita and Yukio Fujiki

      Accepted manuscript online: 18 JAN 2016 06:30AM EST | DOI: 10.1111/tra.12376

      Thumbnail image of graphical abstract

      Mammalian PMPs are thought to insert into peroxisomes post-translationally via the Pex19p- and Pex3p-dependent class I pathway. We analyzed the targeting process of several topologically distinct PMPs to gain more insights into this postulation. We show that PMPs, including ATAD1 that dually localizes to peroxisomes and mitochondria, are translocated to peroxisomes in the form of Pex19p-PMP complexes. Furthermore, we show that targeting is accomplished via the interaction between Pex19p and Pex3p. Our results support the direct import model of mammalian PMPs.

    2. Molecular basis for the interaction between Adaptor Protein Complex 4 (AP4) β4 and its accessory protein, tepsin

      Meredith N. Frazier, Alexandra K. Davies, Markus Voehler, Amy K. Kendall, Georg H. H. Borner, Walter J. Chazin, Margaret S. Robinson and Lauren P. Jackson

      Accepted manuscript online: 12 JAN 2016 02:55AM EST | DOI: 10.1111/tra.12375

      Thumbnail image of graphical abstract

      The adaptor protein (AP) complex family mediates membrane trafficking events, but the molecular mechanisms of the non-clathrin AP4 coat remain poorly understood. We identify a conserved sequence in the AP4 accessory protein, tepsin, that directly interacts with the β4 appendage domain, and we map the tepsin binding site on the β4 surface. Mutations of key residues in the tepsin sequence or on β4 demonstrate their importance for binding both in vitro and in cultured cells. These data provide the first detailed molecular glimpse of how AP4 interacts with an accessory protein.

  8. Traffic Interchanges

    1. Five Questions (with their Answers) on ER-associated Degradation

      Giorgia Brambilla Pisoni and Maurizio Molinari

      Accepted manuscript online: 11 JAN 2016 04:21AM EST | DOI: 10.1111/tra.12373

      Thumbnail image of graphical abstract

      This review focuses on protein destruction, which is, paradoxically, a crucial event for cell and organism survival. It regulates the physiological turnover of proteins and the clearance of faulty biosynthetic products.

      It mainly relies on the intervention of two catabolic machineries, the ubiquitin proteasome system (UPS) and autophagy. Classical ERAD substrates undergo polyubiquitylation and are degraded by cytosolic 26S proteasomes. Misfolded proteins that get into aggregates might enter in autophagosomes for eventual lysosomal destruction. Other proteolytic systems comprise putative intraluminal and intramembrane proteases, tricorn protease-like hydrolases, and calpains.

  9. Original Articles

    1. Nuclear LC3 associates with slowly diffusing complexes that survey the nucleolus

      Lewis J. Kraft, Pallavi Manral, Jacob Dowler and Anne K. Kenworthy

      Accepted manuscript online: 5 JAN 2016 01:17AM EST | DOI: 10.1111/tra.12372

      Thumbnail image of graphical abstract

      A key component of the autophagy pathway, LC3 contributes to both autophagosome formation and cargo selection. LC3 is also present in the nucleus under basal conditions, but the mechanisms that facilitate the nuclear targeting and trafficking of LC3 between the nucleus and cytoplasm are poorly understood. Here, we show that LC3 is retained in the nucleus in association with high molecular weight complexes, and also accesses the nucleolus. In addition, we identify a series of candidate nuclear LC3 interacting proteins.

    2. Ferlins show tissue-specific expression and segregate as plasma membrane/late endosomal or trans-Golgi/recycling ferlins

      Gregory Michael Ian Redpath, Reece Andrew Sophocleous, Lynne Turnbull, Cynthia B Whitchurch and Sandra T Cooper

      Accepted manuscript online: 27 DEC 2015 11:53PM EST | DOI: 10.1111/tra.12370

      Thumbnail image of graphical abstract

      Ferlins are an ancient family of Ca2+-binding, multi-C2 domain vesicle fusion proteins. Of the six human ferlins, mutations in dysferlin cause muscular dystrophy and otoferlin cause deafness. We detail the tissue-distribution, subcellular localization and endocytic trafficking of the human ferlins. Dysferlin and myoferlin, type-I ferlins, localise to the plasma membrane and late endosomes, which display potential for occasional recycling. Otoferlin and Fer1L6, type-II ferlins, localise to dedicated recycling sub-compartments of the trans-Golgi network. We establish that type-I and type-II ferlins segregate into late-endosomal and recycling trans-Golgi compartments.


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