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Edited By: Michael S. Marks, Trina A. Schroer, Robert G. Parton and Sharon A. Tooze
Online ISSN: 1600-0854
Recently Published Articles
- 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
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.
- 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
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.
- 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
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.
- You have free access to this contentDNA-based probes for flow cytometry analysis of endocytosis and recycling
Claire Dumont, Ewa Czuba, Moore Chen, Jose A. Villadangos, Angus P.R. Johnston and Justine D. Mintern
Version of Record online: 7 FEB 2017 | DOI: 10.1111/tra.12466
We demonstrate the utility of a DNA-based specific hybridization internalization probe (SHIP) assay to examine endocytosis and recycling of ligands that bind to receptor proteins using flow cytometry. We monitored endocytosis of membrane-bound transferrin receptor (TFR) and its soluble ligand transferrin (TF) in cell lines and primary cells. We demonstrate that internalization and recycling of holo-TF, and an antibody against the TFR behave differently. SHIP provides a convenient and high-throughput technique for analysis of trafficking of cell surface receptors and ligands.
- 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.