ArticleScience (New York, N.Y.)2015
Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo.
Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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
78 citing papers in PubMed.
- ALS mutations disrupt self-association between the ubiquilin STI1 hydrophobic groove and internal placeholder sequences.The EMBO journal · 2026Article
- Remote on-off switching of protein activity by intrinsically disordered region.Nature structural & molecular biology · 2025Article
- Nucleotide- and metalloid-driven conformational changes in the arsenite efflux ATPase ArsA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- GET3B is involved in chloroplast biogenesis and interacts with the thylakoidal ALB3 and ALB4 insertases.Plant cell reports · 2025Article
- ARMC1 partitions between distinct complexes and assembles MIRO with MTFR to control mitochondrial distribution.Science advances · 2025Article
- FgGET3, an ATPase of the GET Pathway, Is Important for the Development and Virulence ofInternational journal of molecular sciences · 2024Article
- A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024Review
- 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
- The GET insertase exhibits conformational plasticity and induces membrane thinning.Nature communications · 2023Article
- Structures of Get3d reveal a distinct architecture associated with the emergence of photosynthesis.The Journal of biological chemistry · 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
- The Get1/2 insertase forms a channel to mediate the insertion of tail-anchored proteins into the ER.Cell reports · 2023Article
- Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond.International journal of molecular sciences · 2023Review
- Article
- ATP13A1 prevents ERAD of folding-competent mislocalized and misoriented proteins.Molecular cell · 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
- Deciphering the molecular organization of GET pathway chaperones through native mass spectrometry.Biophysical journal · 2022Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Tail-anchored (TA) proteins are a physiologically important class of membrane proteins targeted to the endoplasmic reticulum by the conserved guided-entry of TA proteins (GET) pathway. During transit, their hydrophobic transmembrane domains (TMDs) are chaperoned by the cytosolic targeting factor Get3, but the molecular nature of the functional Get3-TA protein targeting complex remains unknown. We reconstituted the physiologic assembly pathway for a functional targeting complex and showed that it comprises a TA protein bound to a Get3 homodimer. Crystal structures of Get3 bound to different TA proteins showed an α-helical TMD occupying a hydrophobic groove that spans the Get3 homodimer. Our data elucidate the mechanism of TA protein recognition and shielding by Get3 and suggest general principles of hydrophobic domain chaperoning by cellular targeting factors.
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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.