ArticleNature structural & molecular biology2021
Structural insights into metazoan pretargeting GET complexes.
Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Retrograde trafficking inhibitors allosterically trap Get3 to block tail-anchored protein biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Signal recognition particle-dependent secretome in humans.Scientific reports · 2026Article
- ASNA1 is essential for cardiac development and function by regulating tail-anchored protein stability and vesicular transport in cardiomyocytes.PLoS genetics · 2025Article
- A distinct dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo.BMC biology · 2024Article
- A dual role of the conserved PEX19 helix in safeguarding peroxisomal membrane proteins.iScience · 2024Article
- Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad.Nature communications · 2024Article
- The GET insertase exhibits conformational plasticity and induces membrane thinning.Nature communications · 2023Article
- Proteotoxic stresses stimulate dissociation of UBL4A from the tail-anchored protein recognition complex.The Biochemical journal · 2023Article
- The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023Review
- A TAle of Two Pathways: Tail-Anchored Protein Insertion at the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023Review
- Structurally derived universal mechanism for the catalytic cycle of the tail-anchored targeting factor Get3.Nature structural & molecular biology · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Close coordination between chaperones is essential for protein biosynthesis, including the delivery of tail-anchored (TA) proteins containing a single C-terminal transmembrane domain to the endoplasmic reticulum (ER) by the conserved GET pathway. For successful targeting, nascent TA proteins must be promptly chaperoned and loaded onto the cytosolic ATPase Get3 through a transfer reaction involving the chaperone SGTA and bridging factors Get4, Ubl4a and Bag6. Here, we report cryo-electron microscopy structures of metazoan pretargeting GET complexes at 3.3-3.6 Å. The structures reveal that Get3 helix 8 and the Get4 C terminus form a composite lid over the Get3 substrate-binding chamber that is opened by SGTA. Another interaction with Get4 prevents formation of Get3 helix 4, which links the substrate chamber and ATPase domain. Both interactions facilitate TA protein transfer from SGTA to Get3. Our findings show how the pretargeting complex primes Get3 for coordinated client loading and ER targeting.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.