Cover image for Vol. 18 Issue 3

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, Robert G. Parton and Sharon A. Tooze

Online ISSN: 1600-0854


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    1. μ2-Dependent Endocytosis of N-cadherin Is Regulated by β-Catenin to Facilitate Neurite Outgrowth

      Yi-ting Chen and Chin-Yin Tai

      Accepted manuscript online: 22 FEB 2017 12:35AM EST | DOI: 10.1111/tra.12473

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      Synopsis and Graphical Table of Contents:

      Endocytosis of adhesion molecules is required for early neuronal development. Here we identified and characterized the mechanism controlling N-cadherin endocytosis through β-catenin-gated μ2/AP-2 binding to modulate neurite outgrowth.


    1. Global and local mechanisms sustain axonal proteostasis of transmembrane proteins

      Víctor Hugo Cornejo, Alejandro Luarte and Andrés Couve

      Accepted manuscript online: 21 FEB 2017 05:40AM EST | DOI: 10.1111/tra.12472

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      Axonal proteostasis of membrane proteins is a complex phenomenon that involves post-Golgi vesicular transport (solid turquoise arrow and green membrane proteins), local translation/processing/trafficking (solid turquoise arrow and red membrane proteins), supply from supporting cells (dashed turquoise arrow and turquoise membrane proteins), and timely degradation (solid orange arrow). Although some of these mechanisms need further evidence or are currently somewhat speculative, the axon may be considered a system in which global and local phenomena interact to sustain function.

    2. Routes and Mechanisms of Post-Endosomal Cholesterol Trafficking: a Story that Never Ends

      Jie Luo, Luyi Jiang, Hongyuan Yang and Bao-Liang Song

      Accepted manuscript online: 13 FEB 2017 10:55AM EST | DOI: 10.1111/tra.12471

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      Abstract Figure. Post-endosomal cholesterol transport in a mammalian cell. Low-density lipoprotein (LDL) particles are taken up via LDL receptor (LDLR)-mediated endocytosis and delivered from early endosome (EE) to late endosome (LE)/lysosome (LY), during which LDL cholesteryl esters are hydrolyzed by acid lipase (AL) to release free cholesterol. Liberated cholesterol then exits LE/LY and moves to other organelles including the plasma membrane (PM), endoplasmic reticulum (ER), peroxisome (PERO), Golgi and mitochondria. These trafficking processes may involve nonvesicular transport at membrane contact sites formed by two closely apposed organelles. Upon reaching one membrane, cholesterol can be further delivered to another one, for example, the PM-to-ER retrograde cholesterol transport.


    1. ER-to-Golgi Blockade of Nascent Desmosomal Cadherins in SERCA2-inhibited Keratinocytes: Implications for Darier's Disease

      Ning Li, Moonhee Park, Shengxiang Xiao, Zhi Liu and Luis A. Diaz

      Accepted manuscript online: 3 FEB 2017 03:40AM EST | DOI: 10.1111/tra.12470

      Desmosomal cadherins (DC) are Ca2+-dependent transmembrane glycoproteins of desmosomes that are critical in maintaining keratinocyte cohesion. Darier's disease (DD) is an autosomal dominant skin disease characterized by loss of desmosomes/cohesions between keratinocytes. The defective gene in DD is ATP2A2, which encodes SERCA2, a Ca2+-pump located in the endoplasmic reticulum (ER). Here we show that SERCA2 is crucial for ER-to-Golgi transport of nascent DC. Colocalization of DC and ER calnexin is detected in DD epidermis, suggesting that ER retention of DC may contribute to DD pathogenesis.

    2. Beyond attachment: roles of DC-SIGN in dengue virus infection

      Ping Liu, Marc Ridilla, Pratik Patel, Laurie Betts, Emily Gallichotte, Lidea Shahidi, Nancy L. Thompson and Ken Jacobson

      Accepted manuscript online: 27 JAN 2017 08:11AM EST | DOI: 10.1111/tra.12469

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      Graphical Table of Contents

      Whether DC-SIGN functions as merely an attachment factor for dengue virus (DENV) or whether DC-SIGN plays further roles beyond attachment has been controversial. We use mammalian cell culture models, as well as primary dendritic cells, and high resolution, quantitative fluorescence microscopy to track the movements of DC-SIGN and DENV during viral entry. Our results support a model in which DC-SIGN captures DENV and participates, along with a co-receptor, in DENV internalization via clathrin-coated structures and subsequent trafficking to early endosomes.


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