Cover image for Vol. 18 Issue 9

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

Online ISSN: 1600-0854

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Recently Published Articles

  1. You have full text access to this OnlineOpen article
    Two novel effectors of trafficking and maturation of the yeast plasma membrane H+-ATPase

    Yosef Geva, Jonathan Crissman, Eric C. Arakel, Natalia Gómez-Navarro, Silvia G. Chuartzman, Kyle R. Stahmer, Blanche Schwappach, Elizabeth A. Miller and Maya Schuldiner

    Version of Record online: 16 AUG 2017 | DOI: 10.1111/tra.12503

    Thumbnail image of graphical abstract

    Ydl121c (Exp1) and Ykl077w (Psg1) are 2 uncharacterized yeast proteins that mediate the trafficking and maturation of Pma1, the essential plasma-membrane proton ATPase. Exp1 is an ER protein that is packaged into coat protein II (COPII)-vesicles, and whose deletion causes ER retention of Pma1, suggesting that it functions as a cargo receptor. Psg1 physically interacts with Exp1, can be found in the Golgi and coat protein I (COPI) vesicles and causes enhanced vacuolar degradation of Pma1 when absent, consistent with a function in Pma1 sorting. Cleaved forms of Psg1 (N and C) are found in Golgi and COPI, respectively.

  2. An automated quantitative image analysis tool for the identification of microtubule patterns in plants

    Christine Faulkner, Ji Zhou, Alexandre Evrard, Gildas Bourdais, Dan MacLean, Heidrun Häweker, Peter Eckes and Silke Robatzek

    Version of Record online: 16 AUG 2017 | DOI: 10.1111/tra.12505

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    CellArchitect is an automated image analysis tool that quantifies changes to complex, network-like subcellular patterns such as the microtubule cytoskeleton in plants. This tool performs analyses from large image datasets and can distinguish effects induced by different chemicals, which lends itself to identification and characterization of bio-active chemicals. CellArchitect facilitates automated, high throughput quantitative characterisation of cellular responses by image-based screening.

  3. Transport of the alpha subunit of the voltage gated L-type calcium channel through the sarcoplasmic reticulum occurs prior to localization to triads and requires the beta subunit but not Stac3 in skeletal muscles (pages 622–632)

    Jeremy W. Linsley, I-Uen Hsu, Wenjia Wang and John Y. Kuwada

    Version of Record online: 14 AUG 2017 | DOI: 10.1111/tra.12502

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    Subcellular localization of DHPR at triadic junctions in skeletal muscle is required for EC coupling. We find that DHPR is transported via sarcoplasmic membrane to triads independent of microtubules. There appears also to be ER exit sites in the triads and nearby local Golgi outposts. Furthermore, SR trafficking of DHPR to triads is differentially affected in null mutations of Stac3 or DHPRβ, 2 essential components of EC coupling. These findings suggest a model for trafficking of DHPR to the triadic T tubule in wild-type (WT) skeletal muscles whereby DHPRα (α) is transported with DHPRβ (β) in the membrane of the longitudinal SR (L-SR) to the triadic junctional SR (J-SR). DHPR is trafficked from the endoplasmic reticulum exit site (ERES) at the J-SR to local Golgi then to the T tubule at the triads where it is assembled into tetrads with ryanodine receptor 1 (RyR1) and stabilized by Stac3 (S3).

  4. Endoplasmic reticulum is the sorting core facility in the Golgi-lacking protozoan Giardia lamblia (pages 604–621)

    Nahuel Zamponi, Emiliano Zamponi, Gonzalo F. Mayol, Adriana Lanfredi-Rangel, Staffan G. Svärd and María C. Touz

    Version of Record online: 14 AUG 2017 | DOI: 10.1111/tra.12501

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    Regulated protein trafficking in the protozoa Giardia lamblia shows some singularities. (1) After performing its chaperone function, BiP is retained at the ER lumen by the KDELR for further cycles of protein folding. (2) CWP (cyst wall protein) 1-3 are folded and recruited to form the nascent ESVs (encystation-specific vesicles). (3) The COPII-subunits, Sec23 and Sec24, cycle between forming the complex in the ceramide-enriched ERES membrane to its dissociation after vesicle formation. (4) Nascent ESVs go throughout maturation when they traffic to the plasma membrane (PM). ESV: Encystation-specific vesicles. KDELR: KDEL receptor. CWP, cyst wall protein; ERES, ER exit-sites.

  5. Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin (pages 590–603)

    Tara L. Archuleta, Meredith N. Frazier, Anderson E. Monken, Amy K. Kendall, Joel Harp, Airlie J. McCoy, Nicole Creanza and Lauren P. Jackson

    Version of Record online: 14 AUG 2017 | DOI: 10.1111/tra.12499

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    Tepsin is an accessory protein in AP4-coated vesicles, but its biological role remains unknown. Crystal structures of both folded domains (epsin N-terminal homology [ENTH] and VHS/ENTH-like) reveal these domains harbor structural features distinct from other ENTH/ANTH/VHS superfamily proteins. Phylogenetic and comparative genomics data show how tepsin diverged away from other epsins early in evolutionary history. Together these results imply tepsin has diverged away to undertake a distinct biological role.