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Dissecting the molecular organization of the translocon-associated protein complex

Author

Listed:
  • Stefan Pfeffer

    (Max-Planck Institute of Biochemistry)

  • Johanna Dudek

    (Saarland University)

  • Miroslava Schaffer

    (Max-Planck Institute of Biochemistry)

  • Bobby G. Ng

    (Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute)

  • Sahradha Albert

    (Max-Planck Institute of Biochemistry)

  • Jürgen M. Plitzko

    (Max-Planck Institute of Biochemistry)

  • Wolfgang Baumeister

    (Max-Planck Institute of Biochemistry)

  • Richard Zimmermann

    (Saarland University)

  • Hudson H. Freeze

    (Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute)

  • Benjamin D. Engel

    (Max-Planck Institute of Biochemistry)

  • Friedrich Förster

    (Max-Planck Institute of Biochemistry
    Cryo-Electron Microscopy, Bijvoet Center for Biomolecular Research, Utrecht University)

Abstract

In eukaryotic cells, one-third of all proteins must be transported across or inserted into the endoplasmic reticulum (ER) membrane by the ER protein translocon. The translocon-associated protein (TRAP) complex is an integral component of the translocon, assisting the Sec61 protein-conducting channel by regulating signal sequence and transmembrane helix insertion in a substrate-dependent manner. Here we use cryo-electron tomography (CET) to study the structure of the native translocon in evolutionarily divergent organisms and disease-linked TRAP mutant fibroblasts from human patients. The structural differences detected by subtomogram analysis form a basis for dissecting the molecular organization of the TRAP complex. We assign positions to the four TRAP subunits within the complex, providing insights into their individual functions. The revealed molecular architecture of a central translocon component advances our understanding of membrane protein biogenesis and sheds light on the role of TRAP in human congenital disorders of glycosylation.

Suggested Citation

  • Stefan Pfeffer & Johanna Dudek & Miroslava Schaffer & Bobby G. Ng & Sahradha Albert & Jürgen M. Plitzko & Wolfgang Baumeister & Richard Zimmermann & Hudson H. Freeze & Benjamin D. Engel & Friedrich Fö, 2017. "Dissecting the molecular organization of the translocon-associated protein complex," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14516
    DOI: 10.1038/ncomms14516
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    Cited by:

    1. Bethany N. Radford & Xiang Zhao & Tali Glazer & Malcolm Eaton & Danielle Blackwell & Shuhiba Mohammad & Lucas Daniel Lo Vercio & Jay Devine & Tali Shalom-Barak & Benedikt Hallgrimsson & James C. Cross, 2023. "Defects in placental syncytiotrophoblast cells are a common cause of developmental heart disease," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Weimin Li & Angdi Li & Bing Yu & Xiaoxiao Zhang & Xiaoyan Liu & Kate L. White & Raymond C. Stevens & Wolfgang Baumeister & Andrej Sali & Marion Jasnin & Liping Sun, 2024. "In situ structure of actin remodeling during glucose-stimulated insulin secretion using cryo-electron tomography," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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