ArticleScientific reports2017
In search of tail-anchored protein machinery in plants: reevaluating the role of arsenite transporters.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- A distinct dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo.BMC biology · 2024Article
- New Insights into the Chloroplast Outer Membrane Proteome and Associated Targeting Pathways.International journal of molecular sciences · 2022Review
- Looking for a safe haven: tail-anchored proteins and their membrane insertion pathways.Plant physiology · 2021Review
- Genome-wide analysis of Homo sapiens, Arabidopsis thaliana, and Saccharomyces cerevisiae reveals novel attributes of tail-anchored membrane proteins.BMC genomics · 2019Article
- Multiple downy mildew effectors target the stress-related NAC transcription factor LsNAC069 in lettuce.The Plant journal : for cell and molecular biology · 2019Article
- Biogenesis of chloroplast outer envelope membrane proteins.Plant cell reports · 2019Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although the mechanisms underlying selective targeting of tail-anchored (TA) membrane proteins are well established in mammalian and yeast cells, little is known about their role in mediating intracellular membrane trafficking in plant cells. However, a recent study suggested that, in green algae, arsenite transporters located in the cytosol (ArsA1 and ArsA2) control the insertion of TA proteins into the membrane-bound organelles. In the present work, we overproduced and purified these hydrophilic proteins to near homogeneity. The analysis of their catalytic properties clearly demonstrates that C. reinhardtii ArsA proteins exhibit oxyanion-independent ATPase activity, as neither arsenite nor antimonite showed strong effects. Co-expression of ArsA proteins with TA-transmembrane regions showed not only that the former interact with the latter, but that ArsA1 does not share the same ligand specificity as ArsA2. Together with a structural model and molecular dynamics simulations, we propose that C. reinhadtii ArsA proteins are not arsenite transporters, but a TA-protein targeting factor. Further, we propose that ArsA targeting specificity is achieved at the ligand level, with ArsA1 mainly carrying TA-proteins to the chloroplast, while ArsA2 to the endoplasmic reticulum.
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Registered trials
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