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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 and Sharon A. Tooze

Online ISSN: 1600-0854

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  1. 1 - 4
  1. Original Articles

    1. Vesicles are persistent features of different plastids

      Emelie Lindquist, Katalin Solymosi and Henrik Aronsson

      Accepted manuscript online: 12 JUL 2016 09:40PM EST | DOI: 10.1111/tra.12427

      Thumbnail image of graphical abstract

      Vesicles in plastids have been observed repeatedly, suggested to function in thylakoid biogenesis. Previous observations have mainly concerned proplastids and chloroplasts, often being pre-treated to induce formation or inhibit fusion of vesicles. Here we present vesicle-like structures in etio-, etio-chloro-, leuco-, chromo- and desiccoplasts, in addition to both proplastids and chloroplasts. They are here shown without any pre-treatment of plants aiming to enhance vesicle appearance, and in different species (including both C3 and C4 plants), cell types and organs.

    2. Identification of new fungal peroxisomal matrix proteins and revision of the PTS1 consensus

      Christopher Nötzel, Thomas Lingner, Heiner Klingenberg and Sven Thoms

      Accepted manuscript online: 8 JUL 2016 08:30AM EST | DOI: 10.1111/tra.12426

      Thumbnail image of graphical abstract

      The peroxisomal targeting signal type 1 (PTS1) is the prevalent peroxisomal targeting signal. Its current definition, however, is largely incomplete. We have modelled PTS1 by a machine learning approach in yeast. Based on this, we identified two conserved genes encoding novel peroxisomal proteins and we updated the consensus motif to now include all PTS1 proteins in yeast.

  2. Toolbox

    1. Ikarugamycin: a natural product inhibitor of clathrin-mediated endocytosis

      Sarah R. Elkin, Nathaniel W. Oswald, Dana Kim Reed, Marcel Mettlen, John B. McMillan and Sandra L. Schmid

      Accepted manuscript online: 8 JUL 2016 08:30AM EST | DOI: 10.1111/tra.12425

  3. Original Articles

    1. Phosphatidic acid sequesters Sec18p from cis-SNARE complexes to inhibit priming

      Matthew L. Starr, Logan R. Hurst and Rutilio A. Fratti

      Accepted manuscript online: 1 JUL 2016 07:08AM EST | DOI: 10.1111/tra.12423

      Thumbnail image of graphical abstract

      In this study we found that the yeast NSF orthologue Sec18p resides in an inactive pool bound to phosphatidic acid on the vacuolar/lysosomal membrane. The association of Sec18p with phosphatidic acid is disrupted by vacuolar phosphatidic acid phosphatase activity leading to the transfer of Sec18p to cis-SNARE complexes for the priming reaction. In the presence of excess phosphatidic acid or the lack of phosphatidic acid phosphatase activity results in the sequestration of Sec18p away from cis-SNARE complexes.

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