ArticleThe Journal of biological chemistry2014
N-terminal proline-rich domain is required for scrambling activity of human phospholipid scramblases.
Article in The Journal of biological chemistry, 2014. 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, 27 citations in OpenAlex.
- Adverse effects of 6PPD-quinone bioaccumulation at environmentally relevant concentrations on Cyprinus carpio growth and development.Scientific reports · 2026Article
- Phospholipid Scramblase 1 Controls Efficient Neurotransmission and Synaptic Vesicle Retrieval at Cerebellar Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Phospholipid scramblase 1: an essential component of the nephrocyte slit diaphragm.Cellular and molecular life sciences : CMLS · 2024Article
- TargetingVaccines · 2024Review
- Biophysical characterization of the DNA binding motif of human phospholipid scramblase 1.European biophysics journal : EBJ · 2022Article
- Are cysteine residues of human phospholipid scramblase 1 essential for PbEuropean biophysics journal : EBJ · 2021Article
- Identification and characterisation of a phospholipid scramblase in the malaria parasite Plasmodium falciparum.Molecular and biochemical parasitology · 2021Article
- Phylogenetic Analysis and In Vitro Bifunctional Nuclease Assay ofMolecules (Basel, Switzerland) · 2020Article
- Molecular cloning and biochemical characterization of the phospholipid scramblase SCRM-1 from Caenorhabditis elegans.European biophysics journal : EBJ · 2020Article
- Article
- Phospholipid scramblase 1 interacts with influenza A virus NP, impairing its nuclear import and thereby suppressing virus replication.PLoS pathogens · 2018Article
- Identification and characterization of the novel nuclease activity of human phospholipid scramblase 1.BMC biochemistry · 2016Article
- Tubby-like protein superfamily member PLSCR3 functions as a negative regulator of adipogenesis in mouse 3T3-L1 preadipocytes by suppressing induction of late differentiation stage transcription factors.Bioscience reports · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Human phospholipid scramblase 1 (hPLSCR1), a type II integral class membrane protein, is known to mediate bidirectional scrambling of phospholipids in a Ca(2+)-dependent manner. hPLSCR2, a homolog of hPLSCR1 that lacks N-terminal proline-rich domain (PRD), did not show scramblase activity. We attribute this absence of scramblase activity of hPLSCR2 to the lack of N-terminal PRD. Hence to investigate the above hypothesis, we added the PRD of hPLSCR1 to hPLSCR2 (PRD-hPLSCR2) and checked whether scramblase activity was restored. Functional assays showed that the addition of PRD to hPLSCR2 restored scrambling activity, and deletion of PRD in hPLSCR1 (ΔPRD-hPLSCR1) resulted in a lack of activity. These results suggest that PRD is crucial for the function of the protein. The effects of the PRD deletion in hPLSCR1 and the addition of PRD to hPLSCR2 were characterized using various spectroscopic techniques. Our results clearly showed that hPLSCR1 and PRD-hPLSCR2 showed Ca(2+)-dependent aggregation and scrambling activity, whereas hPLSCR2 and ΔPRD-hPLSCR1 did not show aggregation and activity. Thus we conclude that scramblases exhibit Ca(2+)-dependent scrambling activity by aggregation of protein. Our results provide a possible mechanism for phospholipid scrambling mediated by PLSCRs and the importance of PRD in its function and cellular localization.
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