© 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
- You have full text access to this OnlineOpen articleAlphavirus Restriction by IFITM Proteins
Stuart Weston, Stephanie Czieso, Ian J. White, Sarah E. Smith, Rachael S. Wash, Carmen Diaz-Soria, Paul Kellam and Mark Marsh
Version of Record online: 24 JUN 2016 | DOI: 10.1111/tra.12416
IFITM3 can inhibit cellular infection by two alphaviruses, Sindbis and Semliki Forest virus (SFV). IFITM2 has lower antiviral activity, and IFITM1 does not restrict either virus through the endocytic route of infection. IFITM3 does not inhibit SFV binding, internalization into cells, trafficking to endosomes or low pH-induced conformational changes in the E1 fusion protein. However, the viral capsid is not released into the cytosol in IFITM3 expressing cells.
- Distinct Roles for APPL1 and APPL2 in Regulating Toll-like Receptor 4 Signaling in Macrophages
Jeremy C. Yeo, Adam A. Wall, Lin Luo, Nicholas D. Condon and Jennifer L. Stow
Version of Record online: 23 JUN 2016 | DOI: 10.1111/tra.12415
APPLs 1 and 2 are common signaling adaptors but their roles in macrophages are largely uncharacterized. We show that both APPL1 and APPL2 are associated with surface ruffles and macropinocytic membranes in activated macrophages where they contribute to signaling and transcription downstream of the pathogen-stimulated Toll-like receptor, TLR4. The APPLs exert disparate, sometimes opposing regulation that helps to shape the inflammatory cytokine program for innate immune responses.
- Rab35 GTPase: a central regulator of phosphoinositides and F-actin in endocytic recycling and beyond
Kerstin Klinkert and Arnaud Echard
Accepted manuscript online: 21 JUN 2016 10:30PM EST | DOI: 10.1111/tra.12422
In the past ten years, Rab35 has become one of the most studied Rabs involved in a growing number of key cellular functions, including endosomal trafficking, exosome release, phagocytosis, cell migration, immunological synapse formation and neurite outgrowth. In addition, oncogenic activating mutations have been recently found in cancer patients. Here, we provide a comprehensive review on how Rab35 controls these apparently unrelated functions by regulating phosphoinositides and F-actin, both on endosomes and at the plasma membrane.
- BMP2 Transfer to Neighboring Cells and Activation of Signaling
Hamed Alborzinia, Marjan Shaikhkarami, Peter Hortschansky and Stefan Wölfl
Accepted manuscript online: 16 JUN 2016 02:05AM EST | DOI: 10.1111/tra.12420
BMP signaling plays a central role in development and organ homeostasis, and is tightly regulated at various levels. Internalization of BMP2 by cells can provide another layer of regulation. We show that internalized BMP2 is transferred to neighboring cells and can induce BMP signaling. Cell-cell contact increased transfer and enhanced signaling. Noggin blocked signaling but also enhanced transfer. Inhibition of vesicular transport blocked transfer, without clear interference with signaling, suggesting that BMP2 signaling occurs independent of internalization and transfer.
- The HOPS/Class C Vps complex tethers high-curvature membranes via a direct protein-membrane interaction
Ruoya Ho and Christopher Stroupe
Accepted manuscript online: 16 JUN 2016 02:05AM EST | DOI: 10.1111/tra.12421
Here, we show that the HOPS membrane tethering complex can tether highly-curved membranes by binding to these membranes via the ALPS (amphipathic lipid packing sensor) motif in its Vps41p subunit. We propose that this protein-membrane interaction directs the localization of HOPS to the highly-curved “vertex ring” at the edge of the flattened zone of contact between tethered yeast vacuoles.