ArticlePlant physiology2010
The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein.
Article in Plant physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 61 citations in OpenAlex.
- Assembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts.Nature communications · 2026Article
- Alternative proteoforms and proteoform-dependent assemblies in humans and plants.Molecular systems biology · 2024Article
- A molecular atlas of plastid and mitochondrial proteins reveals organellar remodeling during plant evolutionary transitions from algae to angiosperms.PLoS biology · 2024Article
- Selective autophagy regulates chloroplast protein import and promotes plant stress tolerance.The EMBO journal · 2023Article
- The journey of preproteins across the chloroplast membrane systems.Frontiers in physiology · 2023Review
- Functions of autophagy in chloroplast protein degradation and homeostasis.Frontiers in plant science · 2022Review
- Article
- Protein import into chloroplasts and its regulation by the ubiquitin-proteasome system.Biochemical Society transactions · 2020Review
- Origins, function, and regulation of the TOC-TIC general protein import machinery of plastids.Journal of experimental botany · 2020Article
- The TOC GTPase Receptors: Regulators of the Fidelity, Specificity and Substrate Profiles of the General Protein Import Machinery of Chloroplasts.The protein journal · 2019Review
- PhDHS Is Involved in Chloroplast Development in Petunia.Frontiers in plant science · 2019Article
- Chloroplast Degradation: Multiple Routes Into the Vacuole.Frontiers in plant science · 2019Review
- The novel chloroplast outer membrane kinase KOC1 is a required component of the plastid protein import machinery.The Journal of biological chemistry · 2017Article
- Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms.Frontiers in plant science · 2017Review
- A Comprehensive Analysis of Chromoplast Differentiation Reveals Complex Protein Changes Associated with Plastoglobule Biogenesis and Remodeling of Protein Systems in Sweet Orange Flesh.Plant physiology · 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
- Characterization of chloroplast protein import without Tic56, a component of the 1-megadalton translocon at the inner envelope membrane of chloroplasts.Plant physiology · 2015Article
- Oryza sativa Chloroplast Signal Recognition Particle 43 (OscpSRP43) Is Required for Chloroplast Development and Photosynthesis.PloS one · 2015Article
- Emerging roles of protein kinase CK2 in abscisic acid signaling.Frontiers in plant science · 2015Review
- A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts.Frontiers in plant science · 2014Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The translocon at the outer membrane of the chloroplast assists the import of a large class of preproteins with amino-terminal transit sequences. The preprotein receptors Toc159 and Toc33 in Arabidopsis (Arabidopsis thaliana) are specific for the accumulation of abundant photosynthetic proteins. The receptors are homologous GTPases known to be regulated by phosphorylation within their GTP-binding domains. In addition to the central GTP-binding domain, Toc159 has an acidic N-terminal domain (A-domain) and a C-terminal membrane-anchoring domain (M-domain). The A-domain of Toc159 is dispensable for its in vivo activity in Arabidopsis and prone to degradation in pea (Pisum sativum). Therefore, it has been suggested to have a regulatory function. Here, we show that in Arabidopsis, the A-domain is not simply degraded but that it accumulates as a soluble, phosphorylated protein separated from Toc159. However, the physiological relevance of this process is unclear. The data show that the A-domain of Toc159 as well as those of its homologs Toc132 and Toc120 are targets of a casein kinase 2-like activity.
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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.