Dissecting the molecular organization of the translocon-associated protein complex

Pfeffer, Stefan and Dudek, Johanna and Schaffer, Miroslava and Ng, Bobby G. and Albert, Sahradha and Plitzko, Jürgen M. and Baumeister, Wolfgang and Zimmermann, Richard and Freeze, Hudson H. and Engel, Benjamin D. and Förster, Friedrich. (2017) Dissecting the molecular organization of the translocon-associated protein complex. Nature Communications, 8. p. 14516.

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology and Biophysics (Engel)
UniBasel Contributors:Engel, Ben
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Group
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:23 Aug 2022 09:40
Deposited On:23 Aug 2022 09:40

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