ReviewPhotosynthesis research2018
Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.
Review in Photosynthesis research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- Identification of functional pathways and hub genes associated with the heterochronic development of sugarcane axillary buds and sett roots through multi-omics analysis.Frontiers in plant science · 2025Article
- Reliability of plastid and mitochondrial localisation prediction declines rapidly with the evolutionary distance to the training set increasing.PLoS computational biology · 2024Article
- Chloroplast protein translocation pathways and ubiquitin-dependent regulation at a glance.Journal of cell science · 2023Article
- The journey of preproteins across the chloroplast membrane systems.Frontiers in physiology · 2023Review
- The ten amino acids of the oxygen-evolving enhancer of tobacco is sufficient as the peptide residues for protein transport to the chloroplast thylakoid.Plant molecular biology · 2021Article
- Liquid-Liquid Phase Separation Phenomenon on Protein Sorting Within Chloroplasts.Frontiers in physiology · 2021Review
- Measuring the dynamic response of the thylakoid architecture in plant leaves by electron microscopy.Plant direct · 2020Article
- Unprecedented Parallel Photosynthetic Losses in a Heterotrophic Orchid Genus.Molecular biology and evolution · 2019Article
- Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries.Heliyon · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thylakoids are complex sub-organellar membrane systems whose role in photosynthesis makes them critical to life. Thylakoids require the coordinated expression of both nuclear- and plastid-encoded proteins to allow rapid response to changing environmental conditions. Transport of cytoplasmically synthesized proteins to thylakoids or the thylakoid lumen is complex; the process involves transport across up to three membrane systems with routing through three aqueous compartments. Protein transport in thylakoids is accomplished by conserved ancestral prokaryotic plasma membrane translocases containing novel adaptations for the sub-organellar location. This review focuses on the evolutionarily conserved chloroplast twin arginine transport (cpTat) pathway. An overview is provided of known aspects of the cpTat components, energy requirements, and mechanisms with a focus on recent discoveries. Some of the most exciting new studies have been in determining the structural architecture of the membrane complex involved in forming the point of passage for the precursor and binding features of the translocase components. The cpTat system is of particular interest because it transports folded protein domains using only the proton motive force for energy. The implications for mechanism of translocation by recent studies focusing on interactions between membrane Tat components and with the translocating precursor will be discussed.
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