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The SND proteins constitute an alternative targeting route to the endoplasmic reticulum

Author

Listed:
  • Naama Aviram

    (Weizmann Institute of Science)

  • Tslil Ast

    (Weizmann Institute of Science
    †Present address: Broad Institute of Massachusetts Institute of Technology and Harvard, Cambridge, Massachusetts 02114, USA.)

  • Elizabeth A. Costa

    (UCSF California Institute for Quantitative Biomedical Research and Howard Hughes Medical Institute)

  • Eric C. Arakel

    (University Medical Center Göttingen)

  • Silvia G. Chuartzman

    (Weizmann Institute of Science)

  • Calvin H. Jan

    (UCSF California Institute for Quantitative Biomedical Research and Howard Hughes Medical Institute)

  • Sarah Haßdenteufel

    (Saarland University)

  • Johanna Dudek

    (Saarland University)

  • Martin Jung

    (Saarland University)

  • Stefan Schorr

    (Saarland University)

  • Richard Zimmermann

    (Saarland University)

  • Blanche Schwappach

    (University Medical Center Göttingen
    Max-Planck Institute for Biophysical Chemistry)

  • Jonathan S. Weissman

    (UCSF California Institute for Quantitative Biomedical Research and Howard Hughes Medical Institute)

  • Maya Schuldiner

    (Weizmann Institute of Science)

Abstract

Experiments in yeast cells show that three proteins—Snd1, Snd2 and Snd3—provide an alternative pathway for targeting of cellular proteins to the endoplasmic reticulum.

Suggested Citation

  • Naama Aviram & Tslil Ast & Elizabeth A. Costa & Eric C. Arakel & Silvia G. Chuartzman & Calvin H. Jan & Sarah Haßdenteufel & Johanna Dudek & Martin Jung & Stefan Schorr & Richard Zimmermann & Blanche , 2016. "The SND proteins constitute an alternative targeting route to the endoplasmic reticulum," Nature, Nature, vol. 540(7631), pages 134-138, December.
    • Handle: RePEc:nat:nature:v:540:y:2016:i:7631:d:10.1038_nature20169
    DOI: 10.1038/nature20169
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    Cited by:

    1. Melanie A. McDowell & Michael Heimes & Giray Enkavi & Ákos Farkas & Daniel Saar & Klemens Wild & Blanche Schwappach & Ilpo Vattulainen & Irmgard Sinning, 2023. "The GET insertase exhibits conformational plasticity and induces membrane thinning," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Ulrike Zinnall & Miha Milek & Igor Minia & Carlos H. Vieira-Vieira & Simon Müller & Guido Mastrobuoni & Orsalia-Georgia Hazapis & Simone Giudice & David Schwefel & Nadine Bley & Franka Voigt & Jeffrey, 2022. "HDLBP binds ER-targeted mRNAs by multivalent interactions to promote protein synthesis of transmembrane and secreted proteins," Nature Communications, Nature, vol. 13(1), pages 1-21, December.

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