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

Online ISSN: 1600-0854

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Recently Published Articles

  1. Targeting of tail-anchored membrane proteins to subcellular organelles in Toxoplasma gondii

    Leah R. Padgett, Gustavo Arrizabalaga and William J. Sullivan Jr.

    Version of Record online: 17 JAN 2017 | DOI: 10.1111/tra.12464

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    Subcellular localization of tail-anchored (TA) proteins is dependent on targeting sequences within the C-terminus. We performed the first exploration of TA proteins in the phylum Apicomplexa using the protozoan parasite Toxoplasma gondii as a model. We identified 59 putative TA proteins in the Toxoplasma genome and examined the organellar targeting mechanisms for 9 representatives. These findings provide novel insight into this uncharacterized class of proteins in protozoan parasites and how they traffic to different subcellular compartments.

  2. Mitochondrial protein import in trypanosomes: Expect the unexpected

    Anke Harsman and André Schneider

    Version of Record online: 17 JAN 2017 | DOI: 10.1111/tra.12463

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    A comparative analysis of mitochondrial protein import in yeast and trypanosomes, which are only remotely related, reveals an amazing diversity in the composition of the respective machineries. This is surprising since the protein import systems essentially have the same function in all mitochondria. The differences between the import systems provide exciting examples of convergent evolution over large phylogenetic distances.

  3. Distinct complexes of yeast Snx4 family SNX-BARs mediate retrograde trafficking of Snc1 and Atg27

    Mengxiao Ma, Christopher G. Burd and Richard J. Chi

    Version of Record online: 16 JAN 2017 | DOI: 10.1111/tra.12462

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    Live cell imaging of individual yeast endosomes shows that the Snx4 and the Vps5-Vps17 retromer sorting nexins operate concurrently on a maturing endosome. The 3 Snx4 family proteins form 2 functionally distinct heterodimers: Snx4-Atg20 and Snx4-Snx41. Each heterodimer coats an endosome-derived tubule that mediates retrograde sorting of distinct cargo; the v-SNARE, Snc1, is a cargo of the Snx4-Atg20 pathway, and Snx4-Snx41 mediates retrograde sorting of Atg27, an integral membrane protein implicated in selective autophagy.

  4. Editorial process file includedExogenous Lysophospholipids with Large Head Groups Perturb Clathrin-Mediated Endocytosis

    Ieva Ailte, Anne Berit Dyve Lingelem, Audun Sverre Kvalvaag, Simona Kavaliauskiene, Andreas Brech, Gerbrand Koster, Paul Gunnar Dommersnes, Jonas Bergan, Tore Skotland and Kirsten Sandvig

    Accepted manuscript online: 9 JAN 2017 08:15AM EST | DOI: 10.1111/tra.12468

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    Exogenous addition of saturated lysophospholipids with large head groups to cells strongly inhibits clathrin-mediated endocytosis of transferrin: the number of endocytic pits decreases, the lifetime of AP2-positive pits increases and actin dependency is induced. Experiments with optical tweezers show that less force is required to pull membrane tubules outwards, suggesting that insertion of lysophospholipids in the outer leaflet bends the membrane outwards and counteracts formation of invaginations.

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    The C-terminal tails of heterotrimeric kinesin-2 motor subunits directly bind to α-tubulin1: Possible implications for cilia-specific tubulin entry

    Mukul Girotra, Shalini Srivastava, Anuttama Kulkarni, Ayan Barbora, Kratika Bobra, Debnath Ghosal, Pavithra Devan, Amol Aher, Akanksha Jain, Dulal Panda and Krishanu Ray

    Version of Record online: 5 JAN 2017 | DOI: 10.1111/tra.12461

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    Tubulin entry into the cilia and flagella is essential for their growth. The article by Girotra et al suggests that the tail domains of heterotrimeric kinesin-2 motor subunits can selectively bind certain α-tubulin1 isotypes and regulate the entry of tubulin into cilia. The conjecture is supported by extensive binding studies in vitro and tissue-cultured cells using recombinant tail fragments of both Drosophila and mouse orthologues, as well as genetic analysis in Drosophila.