ArticlePlant signaling & behavior2013
The Remorin C-terminal Anchor was shaped by convergent evolution among membrane binding domains.
Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Revealing plasma membrane protein dynamics in living plant cells with single-molecule tracking.Journal of experimental botany · 2025Article
- Identifying candidate genes for sugar accumulation in sugarcane: an integrative approach.BMC genomics · 2024Article
- Genome-Wide Identification of theLife (Basel, Switzerland) · 2024Article
- Identification and characterization of theFrontiers in plant science · 2024Article
- Molecular characterization and expression analysis of theFrontiers in plant science · 2023Article
- Connecting the dots: from nanodomains to physiological functions of REMORINs.Plant physiology · 2021Review
- Comparative proteomics combined with analyses of transgenic plants reveal ZmREM1.3 mediates maize resistance to southern corn rust.Plant biotechnology journal · 2019Article
- REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement.PLoS pathogens · 2018Article
- Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains.eLife · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
StREM1.3 Remorin is a well-established plant raftophilic protein, predominantly associated with sterol- and sphingolipid-rich membrane rafts. We recently identified a C-terminal domain (RemCA) required and sufficient for StREM1.3 anchoring to the plasma membrane. Here, we report a search for homologs and analogs of RemCA domain in publicly available protein sequence and structure databases. We could not identify RemCA homologous domains outside the Remorin family but we identified domains sharing bias in amino-acid composition and predicted structural fold with RemCA in bacterial, viral and animal proteins. These results suggest that RemCA emerged by convergent evolution among unrelated membrane binding domain.
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Registered trials
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