© 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
- 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.
- 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
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.
- 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
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.
- 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
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.