© John Wiley & Sons A/S. Published by John Wiley & Sons Ltd
Edited By: Michael S. Marks, Trina A. Schroer, Tom H. Stevens and Sharon A. Tooze
Online ISSN: 1600-0854
ORIGINAL ARTICLE: Phosphatidylinositol 3,5-Bisphosphate-Rich Membrane Domains in Endosomes and Lysosomes
ORIGINAL ARTICLE: The Sec1/Munc18 Protein Groove Plays a Conserved Role in Interaction with Sec9p/SNAP-25
ORIGINAL ARTICLE: Phosphorylation of αSNAP is Required for Secretory Organelle Biogenesis in Toxoplasma gondii
REVIEW: The Crossroads of Synaptic Growth Signaling, Membrane Traffic and Neurological Disease: Insights from Drosophila
Recently Published Articles
- Calnuc Function in Endosomal Sorting of Lysosomal Receptors
Heidi Larkin, Santiago Costantino, Matthew N. J. Seaman and Christine Lavoie
Article first published online: 12 FEB 2016 | DOI: 10.1111/tra.12374
Calnuc is a ubiquitous Ca2+-binding protein whose function is poorly characterized. In this study, we demonstrate that Calnuc plays a role in the endosome-to-trans-Golgi network (TGN) retrograde transport of the lysosomal receptors cationic-independent mannose-6-phosphate receptor (CI-MPR) and Sortilin through the activation and membrane association of Rab7, a small G protein required for the endosomal recruitment of retromers.
- Differential Targeting of SLC30A10/ZnT10 Heterodimers to Endolysosomal Compartments Modulates EGF-Induced MEK/ERK1/2 Activity
Yitong Zhao, Rafaela G. Feresin, Juan M. Falcon-Perez and Gloria Salazar
Article first published online: 12 FEB 2016 | DOI: 10.1111/tra.12371
Zinc transporters (ZnTs) transport zinc into subcellular compartments to prevent zinc toxicity. The regulation of the function of the ZnTs, particularly the role of dimerization and heterodimerization in the endocytic pathway, is incompletely understood. Here, we focused on ZnT10, one of the least studied transporters, to show that ZnT10 forms heterodimers with ZnT2, ZnT3 and ZnT4 in endosomes and lysosomes and that ZnT3/ZnT10 heterodimers modulate epidermal growth factor receptor (EGF-R) signaling by upregulating mitogen-activated protein kinase kinase/extracellular signal-regulated kinase 1/2 phosphorylation in response to EGF.
- HCMV Induces Macropinocytosis for Host Cell Entry in Fibroblasts
Stefanie Hetzenecker, Ari Helenius and Magdalena Anna Krzyzaniak
Article first published online: 11 FEB 2016 | DOI: 10.1111/tra.12355
Human cytomegalovirus (HCMV) is a major contributor to disease in newborns and immunosuppressed patients. To date, treatment options are limited. Here we show that HCMV enters primary human fibroblasts by macropinocytosis. Because macropinocytosis is the HCMV entry route in endothelial, epithelial and dendritic cells, this entry mechanism is likely in most relevant cell types. In addition, we found that HCMV induces the formation of circular dorsal ruffles (CDRs). CDRs are commonly observed in primary cells during macropinocytosis but have not previously been observed after virus stimulation.
- 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
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.
- 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
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.