ArticleThe Journal of biological chemistry2009
Toc receptor dimerization participates in the initiation of membrane translocation during protein import into chloroplasts.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 34 citations in OpenAlex.
- Single-molecule fluorescence and cross-linking reveal ligand-gated Toc34 oligomerization dynamics.Biophysical journal · 2026Article
- New Insights into the Chloroplast Outer Membrane Proteome and Associated Targeting Pathways.International journal of molecular sciences · 2022Review
- Molecular Topology of the Transit Peptide during Chloroplast Protein Import.The Plant cell · 2018Article
- Chloroplast Preproteins Bind to the Dimer Interface of the Toc159 Receptor during Import.Plant physiology · 2017Article
- A geminivirus betasatellite damages the structural and functional integrity of chloroplasts leading to symptom formation and inhibition of photosynthesis.Journal of experimental botany · 2015Article
- New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Journal of molecular biology · 2015Review
- Border control: selectivity of chloroplast protein import and regulation at the TOC-complex.Frontiers in plant science · 2014Review
- Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane.Frontiers in plant science · 2014Review
- Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33.The Biochemical journal · 2011Article
- Tail-anchored membrane proteins: exploring the complex diversity of tail-anchored-protein targeting in plant cells.Plant cell reports · 2011Review
- Energetic manipulation of chloroplast protein import and the use of chemical cross-linkers to map protein-protein interactions.Methods in molecular biology (Clifton, N.J.) · 2011Article
- Common ground for protein translocation: access control for mitochondria and chloroplasts.Nature reviews. Molecular cell biology · 2011Review
- The molecular basis for distinct pathways for protein import into Arabidopsis chloroplasts.The Plant cell · 2010Article
- Distinct pathways mediate the sorting of tail-anchored proteins to the plastid outer envelope.PloS one · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The post-translational import of nucleus-encoded preproteins into chloroplasts occurs through multimeric translocons in the outer (Toc) and inner (Tic) membranes. The high fidelity of the protein import process is maintained by specific recognition of the transit peptide of preproteins by the coordinate activities of two homologous GTPase Toc receptors, Toc34 and Toc159. Structural and biochemical studies suggest that dimerization of the Toc receptors functions as a component of the mechanism to control access of preproteins to the membrane translocation channel of the translocon. We show that specific mutations that disrupted receptor dimerization in vitro reduced the rate of protein import in transgenic Arabidopsis compared with the wild type receptor. The mutations did not affect the GTPase activities of the receptors. Interestingly, these mutations did not decrease the initial preprotein binding at the receptors, but they reduced the efficiency of the transition from preprotein binding to membrane translocation. These data indicate that dimerization of receptors has a direct role in protein import and support a hypothesis in which receptor-receptor interactions participate in the initiation of membrane translocation of chloroplast preproteins as part of the molecular mechanism of GTP-regulated protein import.
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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.