Traffic

Cover image for Vol. 18 Issue 10

Edited By: Michael S. Marks, Trina A. Schroer, Robert G. Parton and Sharon A. Tooze

Online ISSN: 1600-0854

Recently Published Issues

See all

Virtual Issues

Advances in Cell Biology in China

Advances in Cell Biology in China
View this issue

Celebrating the Contributions of Ari Helenius

Celebrating the Contributions of Ari Helenius
View this issue

Virtual Issue Toolbox

Toolbox
View this issue

Chemical and Immunological Synapses"

Chemical and Immunological Synapses
View this issue

Recently Published Articles

  1. Nup42 and IP6 coordinate Gle1 stimulation of Dbp5/DDX19B for mRNA export in yeast and human cells

    Rebecca L. Adams, Aaron C. Mason, Laura Glass, Aditi and Susan R. Wente

    Version of Record online: 16 OCT 2017 | DOI: 10.1111/tra.12526

    Thumbnail image of graphical abstract

    Export of mRNA through nuclear pore complexes requires Mex67/Mtr2 export factors to bind both mRNA-bound proteins (Nab2) and nucleoporins (Nups) with FG domains, followed by terminal removal of Mex67/Mtr2/Nab2 through activation of Dbp5 DEAD-box ATPase by Gle1-IP6 at the cytoplasmic face. Adams et al. demonstrate that Nup42 binds Gle1 at a distinct interface to enhance stimulation of Dbp5. Human mRNA export requires both Nup42-hGle1B and IP6-hGle1B interaction. This work reveals mechanisms for spatiotemporal coordination of Gle1-Dbp5 activity with disease implications.

  2. Recruitment of 7SL RNA to Assembling HIV-1 Virus-Like Particles

    Michelle S. Itano, Helene Arnion, Sandra L. Wolin and Sanford M. Simon

    Accepted manuscript online: 16 OCT 2017 08:51AM EST | DOI: 10.1111/tra.12536

    Thumbnail image of graphical abstract

    HIV-1 infection and the associated disease AIDS are a major cause of human death worldwide with no vaccine or cure available. The assembly of virus particles involves numerous host and viral proteins that are potential therapeutic targets. We used high resolution microscopy techniques to investigate how the virus selectively incorporates a noncoding host RNA into virions budding from an infected cell. We show that 7SL RNA interacts with viral Gag proteins in the cytosol and arrives and accumulates with Gag at sites of viral assembly.

  3. V1b vasopressin receptor trafficking and signaling : role of arrestins, G proteins and Src kinase

    Sanja Perkovska, Catherine Méjean, Mohammed Akli Ayoub, Juan Li, Floriane Hemery, Maithé Corbani, Nadine Laguette, Maria-Angeles Ventura, Hélène Orcel, Thierry Durroux, Bernard Mouillac and Christiane Mendre

    Accepted manuscript online: 16 OCT 2017 08:37AM EST | DOI: 10.1111/tra.12535

    Thumbnail image of graphical abstract

    Molecular mechanisms of the vasopressin receptor V1b subtype (V1bR) trafficking and function were investigated. Both β-arrestin-1 and 2 play a fundamental role in internalization and recycling of V1bR with rapid and transient V1bR–arrestin interaction via V1bR C-terminus in a phosphorylation-independent manner. In parallel, V1bR MAP kinase activation is dependent on arrestins and Src-kinase but not on G-proteins. Interestingly, Src kinase interacts with V1bR at the plasma membrane (PM) at basal state and dissociates when receptor internalization occurs.

  4. SNARE proteins in membrane trafficking

    Tuanlao Wang, Liangcheng Li and Wanjin Hong

    Version of Record online: 10 OCT 2017 | DOI: 10.1111/tra.12524

    Thumbnail image of graphical abstract

    SNAREs are the core machinery mediating membrane fusion. The recent studies using biophysical methods and in vitro single molecule analysis provide mechanistic insight of fusion events mediated by SNARE proteins.

  5. Structural insights into the nuclear import of the histone acetyltransferase MOF by importin α1

    Weili Zheng, Rui Wang, Xi Liu, Siyu Tian, Benqiang Yao, Ang Chen, Shikai Jin and Yong Li

    Accepted manuscript online: 9 OCT 2017 09:51AM EST | DOI: 10.1111/tra.12534

    Thumbnail image of graphical abstract

    SYNOPSIS STATEMENT

    The function of the histone acetyltransferase MOF is critical for many biological processes. However, the structural or functional mechanisms of the nucleocytoplasmic transport of MOF remain elusive. We identified novel importin α1-specific nuclear localization signals in the N-terminal of human MOF and revealed a unique binding mode of MOF, further emphasizing the diversity and specificity of the cargo-NLS-importin nuclear import system. Our structural studies will be of great importance in understanding the functional regulation of MOF in various biological processes.

SEARCH

SEARCH BY CITATION