Cover image for Vol. 16 Issue 9

Accepted Articles (Accepted, unedited articles published online and citable. The final edited and typeset version of record will appear in future.)

Edited By: Michael S. Marks, Trina A. Schroer, Tom H. Stevens, Sharon A. Tooze

Online ISSN: 1600-0854


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  1. Original Articles

    1. Distinct trafficking of cell surface and endosomal TIM-1 to the immune synapse

      Meriem Echbarthi, Manuela Zonca, Rachel Mellwig, Yannick Schwab, Gerardo G. Kaplan, Rosemarie H. DeKruyff, Pedro Roda-Navarro and Jose M. Casasnovas

      Accepted manuscript online: 31 AUG 2015 05:00AM EST | DOI: 10.1111/tra.12329

      Thumbnail image of graphical abstract

      The T cell costimulatory molecule TIM-1 sorts mainly to endosomes in lymphoid cells. At difference from the cell surface protein, endosomal TIM-1 translocates to the immune synapse (IS), where it can contribute to antigen-dependent T cell costimulation. TIM-1 ligands increase the amount of cell surface protein, preventing its traffic to the IS. The bipolar sorting of TIM-1 observed during IS formation is determined by differences in its subcellular location, and probably modulates antigen-driven immune responses.

    2. Distinct temporal regulation of RET isoform internalization: roles of clathrin and AP2

      Mathieu JF Crupi, Piriya Yoganathan, Leslie N Bone, Eric Lian, Andrew Fetz, Costin N Antonescu and Lois M Mulligan

      Accepted manuscript online: 25 AUG 2015 04:13AM EST | DOI: 10.1111/tra.12315

      Thumbnail image of graphical abstract

      The RET receptor tyrosine kinase is expressed as two major isoforms, each with important but distinct developmental roles. Here, we show that regulation of cell membrane levels of activated RET isoforms requires clathrin, and direct interactions with the clathrin adaptor AP2, but not caveolin. Our results demonstrate that the ligand-activated RET51 isoform is recruited more rapidly and abundantly into clathrin-coated pits for internalization than the RET9 isoform, indicating that important functional differences between RET isoforms occur early in the intracellular trafficking process.

    3. Endocytosis of ubiquitylation-deficient EGF receptor mutants via clathrin coated pits is mediated by ubiquitylation

      Arola Fortian, Lai Kuan Dionne, Sun Hae Hong, Woong Kim, Steven P. Gygi, Simon Watkins and Alexander Sorkin

      Accepted manuscript online: 7 AUG 2015 12:28AM EST | DOI: 10.1111/tra.12314

      Thumbnail image of graphical abstract

      We used RNA interference screen, mass-spectrometry and fluorescence microscopy to demonstrate that endocytosis of ubiquitylation-deficient mutants of the EGF receptor via clathrin coated pits is mediated by ubiquitylation. The model of EGF receptor endocytosis is proposed whereby two redundant mechanisms involving ubiquitylation and receptor interactions with AP-2 contribute to EGF receptor endocytosis in a stochastic fashion.

    4. Functional roles of N-linked glycosylation of human matrix metalloproteinase 9

      Tyler Duellman, John Burnett and Jay Yang

      Accepted manuscript online: 24 JUL 2015 04:24AM EST | DOI: 10.1111/tra.12312

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      Matrix metalloproteinase-9 (MMP-9) is a secreted endoproteinase with two N-glycosylation sites at residues N38 and N120. Using bimolecular fluorescence complementation, co-immunoprecipitation, fluorescence microscopy, and extensive site-directed mutagenesis we identified the indispensible roles of both N-glycosylation sites for the secretion of MMP-9. The N38-glycosylation deficient MMP-9 revealed a novel polypeptide-binding domain that interacted with calreticulin dependent on the molecular volume of the exposed amino acid. The N120-glycosylation deficient MMP-9 resulted in reduced secretion stemming from a strong interaction with calreticulin.

    5. Subcellular Distribution of NTL Transcription Factors in Arabidopsis thaliana

      Mingwei Liang, Hongjuan Li, Fang Zhou, Huiyong Li, Jin Liu, Yi Hao, Yingdian Wang, Heping Zhao and Shengcheng Han

      Accepted manuscript online: 21 JUL 2015 10:02PM EST | DOI: 10.1111/tra.12311

      NTLs are a class of NAC transcription factors containing a transmembrane domain at their C-terminus. Using a transient transformation approach in Arabidopsis mesophyll protoplasts we showed that twelve NTLs, with the exception of NTL11 and NTL5, are anchored to the ER membrane. Furthermore, the N-terminal NAC domain and the regulation region of NTLs were proved to be responsible for NTLs entering the nucleus. These results indicated that proteolytic activation of NTLs is a regulatory scheme active in plants during various stress situations

  2. Reviews

    1. Mechanisms Regulating Protein Localization

      Nicholas C. Bauer, Paul W. Doetsch and Anita H. Corbett

      Accepted manuscript online: 14 JUL 2015 08:56AM EST | DOI: 10.1111/tra.12310

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      One rapid and efficient mechanism for regulation of protein function is targeted localization. Moving an active protein into a target compartment avoids the expensive need for new protein synthesis. Furthermore, this mode of regulation is rapidly reversible. This review provides an overview of intracellular targeting pathways and then presents mechanisms by which regulation of localization is achieved. Pathways covered in detail include nucleocytoplasmic and mitochondrial transport with more general overviews of chloroplast, peroxisomal, ciliary, endomembrane, and vesicular transport.


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