ArticleThe Journal of biological chemistry2010
Determinants for stop-transfer and post-import pathways for protein targeting to the chloroplast inner envelope membrane.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- Targeting signals required for protein sorting to sub-chloroplast compartments.Plant cell reports · 2024Review
- The N-region sequence context impacts the chloroplast import efficiency of multi-TMD protein.Plant molecular biology · 2024Article
- MFP1 defines the subchloroplast location of starch granule initiation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Chloroplast protein translocation pathways and ubiquitin-dependent regulation at a glance.Journal of cell science · 2023Article
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- Go your own way: membrane-targeting sequences.Plant physiology · 2021Article
- Liquid-Liquid Phase Separation Phenomenon on Protein Sorting Within Chloroplasts.Frontiers in physiology · 2021Review
- Engineered Accumulation of Bicarbonate in Plant Chloroplasts: Known Knowns and Known Unknowns.Frontiers in plant science · 2021Review
- Protein import into chloroplasts and its regulation by the ubiquitin-proteasome system.Biochemical Society transactions · 2020Review
- Genome-wide analysis of Homo sapiens, Arabidopsis thaliana, and Saccharomyces cerevisiae reveals novel attributes of tail-anchored membrane proteins.BMC genomics · 2019Article
- MaizeThe Journal of cell biology · 2019Article
- Evolution of protein transport to the chloroplast envelope membranes.Photosynthesis research · 2018Review
- MCD1 Associates with FtsZ Filaments via the Membrane-Tethering Protein ARC6 to Guide Chloroplast Division.The Plant cell · 2018Article
- Evolution and Design Principles of the Diverse Chloroplast Transit Peptides.Molecules and cells · 2018Review
- Prolines in Transit Peptides Are Crucial for Efficient Preprotein Translocation into Chloroplasts.Plant physiology · 2018Article
- Sorting of SEC translocase SCY components to different membranes in chloroplasts.Journal of experimental botany · 2017Article
- Setting sub-organellar sights: accurate targeting of multi-transmembrane-domain proteins to specific chloroplast membranes.Journal of experimental botany · 2017Article
- Suppressors of the Chloroplast Protein Import MutantThe Plant cell · 2017Article
- Identification of Putative Substrates of SEC2, a Chloroplast Inner Envelope Translocase.Plant physiology · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The inner envelope membrane (IEM) of the chloroplast plays key roles in controlling metabolite transport between the organelle and cytoplasm and is a major site of lipid and membrane synthesis within the organelle. IEM biogenesis requires the import and integration of nucleus-encoded membrane proteins. Previous reports have led to the conclusion that membrane proteins are inserted into the IEM during protein import from the cytoplasm via a stop-transfer mechanism or are completely imported into the stroma and then inserted into the IEM in a post-import mechanism. In this study, we examined the determinants for each pathway by comparing the targeting of APG1 (albino or pale green mutant 1), an example of a stop-transfer substrate, and atTic40, an example of a post-import substrate. We show that the APG1 transmembrane domain is sufficient to direct stop-transfer insertion. The APG1 transmembrane domain also functions as a topology determinant. We also show that the ability of the post-import signals within atTic40 to target proteins to the IEM is dependent upon their context within the full protein sequence. In the incorrect context, the atTic40 signals can behave as stop-transfer signals or fail to target fusion proteins to the IEM. These data suggest that the post-import pathway signals are complex and have evolved to avoid stop-transfer insertion.
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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.