ArticleProceedings of the National Academy of Sciences of the United States of America2013
Precise timing of ATPase activation drives targeting of tail-anchored proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 58 citations in OpenAlex.
- Retrograde trafficking inhibitors allosterically trap Get3 to block tail-anchored protein biogenesis.bioRxiv : the preprint server for biology · 2026Article
- ASNA1 is essential for cardiac development and function by regulating tail-anchored protein stability and vesicular transport in cardiomyocytes.PLoS genetics · 2025Article
- The formation of chaperone-rich GET bodies depends on the tetratricopeptide repeat region of Sgt2 and is reversed by NADH.Journal of cell science · 2025Article
- A distinct dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo.BMC biology · 2024Article
- Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad.Nature communications · 2024Article
- Structures of Get3d reveal a distinct architecture associated with the emergence of photosynthesis.The Journal of biological chemistry · 2023Article
- A TAle of Two Pathways: Tail-Anchored Protein Insertion at the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023Review
- The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023Review
- Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond.International journal of molecular sciences · 2023Review
- From guide to guard-activation mechanism of the stress-sensing chaperone Get3.Molecular cell · 2022Article
- Structurally derived universal mechanism for the catalytic cycle of the tail-anchored targeting factor Get3.Nature structural & molecular biology · 2022Article
- Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022Review
- The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Structural insights into metazoan pretargeting GET complexes.Nature structural & molecular biology · 2021Article
- Subunit cooperation in the Get1/2 receptor promotes tail-anchored membrane protein insertion.The Journal of cell biology · 2021Article
- Endoplasmic reticulum membrane receptors of the GET pathway are conserved throughout eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Two interacting ATPases protectJournal of bacteriology · 2020Article
- Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade.The Journal of biological chemistry · 2019Review
- The Ways of Tails: the GET Pathway and more.The protein journal · 2019Review
- A Chaperone Lid Ensures Efficient and Privileged Client Transfer during Tail-Anchored Protein Targeting.Cell reports · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The localization of tail-anchored (TA) proteins, whose transmembrane domain resides at the extreme C terminus, presents major challenges to cellular protein targeting machineries. In eukaryotic cells, the highly conserved ATPase, guided entry of tail-anchored protein 3 (Get3), coordinates the delivery of TA proteins to the endoplasmic reticulum. How Get3 uses its ATPase cycle to drive this fundamental process remains unclear. Here, we establish a quantitative framework for the Get3 ATPase cycle and show that ATP specifically induces multiple conformational changes in Get3 that culminate in its ATPase activation through tetramerization. Further, upstream and downstream components actively regulate the Get3 ATPase cycle to ensure the precise timing of ATP hydrolysis in the pathway: the Get4/5 TA loading complex locks Get3 in the ATP-bound state and primes it for TA protein capture, whereas the TA substrate induces tetramerization of Get3 and activates its ATPase reaction 100-fold. Our results establish a precise model for how Get3 harnesses the energy from ATP to drive the membrane localization of TA proteins and illustrate how dimerization-activated nucleotide hydrolases regulate diverse cellular processes.
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Registered trials
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.