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Cover image for Vol. 18 Issue 8

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

Online ISSN: 1600-0854

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Advances in Cell Biology in China

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Celebrating the Contributions of Ari Helenius

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Chemical and Immunological Synapses"

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Recently Published Articles

  1. 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

    Accepted manuscript online: 20 JUL 2017 10:05AM EST | DOI: 10.1111/tra.12503

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    Synopsis

    Ydl121c (Exp1) and Ykl077w (Psg1) are two 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 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 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. Transport of the alpha subunit of the 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

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

    Accepted manuscript online: 11 JUL 2017 11:00AM EST | DOI: 10.1111/tra.12502

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    Synopsis

    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, two essential components of EC coupling. These findings suggest a model for trafficking of DHPR to the triadic T-Tubule in wildtype (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).

  3. The ER is the sorting core facility in the Golgi-lacking protozoan Giardia lamblia

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

    Accepted manuscript online: 11 JUL 2017 10:30AM EST | DOI: 10.1111/tra.12501

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    Synopsis

    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.

  4. Sorting without a Golgi complex

    Maria C. Touz and Nahuel Zamponi

    Accepted manuscript online: 11 JUL 2017 10:15AM EST | DOI: 10.1111/tra.12500

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    SYNOPSIS

    Recently, numerous examples of reductive evolution have challenged the general notion that evolution proceeds toward greater complexity both at the organismal and genomic level. The Giardia genus represents a good example of unicellular organisms that have seen reduction of their internal complexity, losing many key eukaryotic organelles such as mitochondria and Golgi. Strikingly, in the absence of a Golgi complex, the ER commands constitutive (1), lysosomal (2), and regulated (3) protein sorting.

  5. Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin

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

    Accepted manuscript online: 10 JUL 2017 04:15AM EST | DOI: 10.1111/tra.12499

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    Synopsis statement

    Tepsin is an accessory protein in AP4 coated vesicles, but its biological role remains unknown. Crystal structures of both folded domains (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.

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