ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structural insights into tail-anchored protein binding and membrane insertion by Get3.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 107 citations in OpenAlex.
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- GET3B is involved in chloroplast biogenesis and interacts with the thylakoidal ALB3 and ALB4 insertases.Plant cell reports · 2025Article
- A distinct dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo.BMC biology · 2024Article
- The GET insertase exhibits conformational plasticity and induces membrane thinning.Nature communications · 2023Article
- The GET pathway serves to activate Atg32-mediated mitophagy by ER targeting of the Ppg1-Far complex.Life science alliance · 2023Article
- A TAle of Two Pathways: Tail-Anchored Protein Insertion at the Endoplasmic Reticulum.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
- Identification of C. elegans ASNA-1 domains and tissue requirements that differentially influence platinum sensitivity and growth control.PLoS genetics · 2022Article
- 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
- Regulated targeting of the monotopic hairpin membrane protein Erg1 requires the GET pathway.The Journal of cell 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
- Capture and delivery of tail-anchored proteins to the endoplasmic reticulum.The Journal of cell biology · 2021Review
- Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily.Nature structural & molecular biology · 2021Review
- 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
- Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade.The Journal of biological chemistry · 2019Review
- A trap mutant reveals the physiological client spectrum of TRC40.Journal of cell science · 2019Article
- The Ways of Tails: the GET Pathway and more.The protein journal · 2019Review
7 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tail-anchored (TA) membrane proteins are involved in a variety of important cellular functions, including membrane fusion, protein translocation, and apoptosis. The ATPase Get3 (Asna1, TRC40) was identified recently as the endoplasmic reticulum targeting factor of TA proteins. Get3 consists of an ATPase and alpha-helical subdomain enriched in methionine and glycine residues. We present structural and biochemical analyses of Get3 alone as well as in complex with a TA protein, ribosome-associated membrane protein 4 (Ramp4). The ATPase domains form an extensive dimer interface that encloses 2 nucleotides in a head-to-head orientation and a zinc ion. Amide proton exchange mass spectrometry shows that the alpha-helical subdomain of Get3 displays considerable flexibility in solution and maps the TA protein-binding site to the alpha-helical subdomain. The non-hydrolyzable ATP analogue AMPPNP-Mg(2+)- and ADP-Mg(2+)-bound crystal structures representing the pre- and posthydrolysis states are both in a closed form. In the absence of a TA protein cargo, ATP hydrolysis does not seem to be possible. Comparison with the ADP.AlF(4)(-)-bound structure representing the transition state (Mateja A, et al. (2009) Nature 461:361-366) indicates how the presence of a TA protein is communicated to the ATP-binding site. In vitro membrane insertion studies show that recombinant Get3 inserts Ramp4 in a nucleotide- and receptor-dependent manner. Although ATP hydrolysis is not required for Ramp4 insertion per se, it seems to be required for efficient insertion. We postulate that ATP hydrolysis is needed to release Get3 from its receptor. Taken together, our results provide mechanistic insights into posttranslational targeting of TA membrane proteins by Get3.
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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.