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Title | Molecular basis of the TRAP complex function in ER protein biogenesis. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 30, Issue 6, Page 770-777, Year 2023 |
Publish date | May 11, 2023 |
Authors | Mateusz Jaskolowski / Ahmad Jomaa / Martin Gamerdinger / Sandeep Shrestha / Marc Leibundgut / Elke Deuerling / Nenad Ban / |
PubMed Abstract | The translocon-associated protein (TRAP) complex resides in the endoplasmic reticulum (ER) membrane and interacts with the Sec translocon and the ribosome to facilitate biogenesis of secretory and ...The translocon-associated protein (TRAP) complex resides in the endoplasmic reticulum (ER) membrane and interacts with the Sec translocon and the ribosome to facilitate biogenesis of secretory and membrane proteins. TRAP plays a key role in the secretion of many hormones, including insulin. Here we reveal the molecular architecture of the mammalian TRAP complex and how it engages the translating ribosome associated with Sec61 translocon on the ER membrane. The TRAP complex is anchored to the ribosome via a long tether and its position is further stabilized by a finger-like loop. This positions a cradle-like lumenal domain of TRAP below the translocon for interactions with translocated nascent chains. Our structure-guided TRAP mutations in Caenorhabditis elegans lead to growth deficits associated with increased ER stress and defects in protein hormone secretion. These findings elucidate the molecular basis of the TRAP complex in the biogenesis and translocation of proteins at the ER. |
External links | Nat Struct Mol Biol / PubMed:37170030 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.5 Å |
Structure data | EMDB-16232, PDB-8btk: |
Chemicals | ChemComp-SPD: ChemComp-SPM: ChemComp-MG: ChemComp-GTP: ChemComp-AAC: ChemComp-ZN: |
Source |
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Keywords | TRANSLOCASE / ER targeting / protein translocation / ER protein biogenesis |