ArticleThe Journal of biological chemistry2011
Structure and mechanism of the saposin-like domain of a plant aspartic protease.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Rapidly evolving aphid gall effector proteins exhibit saposin-like folds.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Alternative splicing serves as a molecular strategy for saliva evolution and diversification in an endoparasitoid, Pteromalus puparum.BMC genomics · 2026Article
- Rapidly evolving aphid gall effector proteins exhibit saposin-like folds.bioRxiv : the preprint server for biology · 2026Article
- Shifting Routes: Plant-Specific Insert Trafficking and Function in Arabidopsis Seedlings Under Abiotic Stress.Plant direct · 2025Article
- Interaction Dynamics of Plant-Specific Insert Domains fromMolecules (Basel, Switzerland) · 2024Article
- The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.Frontiers in plant science · 2023Article
- Genome-Wide Analyses of Aspartic Proteases on Potato Genome (Plants (Basel, Switzerland) · 2022Article
- Quantitative Studies on the Interaction between Saposin-like Proteins and Synthetic Lipid Membranes.Methods and protocols · 2022Article
- Insights into the mechanism of membrane fusion induced by the plant defense element, plant-specific insert.The Journal of biological chemistry · 2020Article
- PSI relieves the pressure of membrane fusion.The Journal of biological chemistry · 2020Article
- The Droserasin 1 PSI: A Membrane-Interacting Antimicrobial Peptide from the Carnivorous PlantBiomolecules · 2020Article
- The role of disulfide bonds in a Solanum tuberosum saposin-like protein investigated using molecular dynamics.PloS one · 2020Article
- Protein Structure Insights into the Bilayer Interactions of the Saposin-Like Domain of Solanum tuberosum Aspartic Protease.Scientific reports · 2017Article
- Characterization of secondary structure and lipid binding behavior of N-terminal saposin like subdomain of human Wnt3a.Archives of biochemistry and biophysics · 2017Article
- Novel proteases from the genome of the carnivorous plant Drosera capensis: Structural prediction and comparative analysis.Proteins · 2016Article
- Understanding the structural basis of substrate recognition by Plasmodium falciparum plasmepsin V to aid in the design of potent inhibitors.Scientific reports · 2016Article
- Article
- Establishing the yeast Kluyveromyces lactis as an expression host for production of the saposin-like domain of the aspartic protease cirsin.Applied and environmental microbiology · 2014Article
- Structure-function correlations of pulmonary surfactant protein SP-B and the saposin-like family of proteins.European biophysics journal : EBJ · 2013Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Many plant aspartic proteases contain an additional sequence of ~100 amino acids termed the plant-specific insert, which is involved in host defense and vacuolar targeting. Similar to all saposin-like proteins, the plant-specific insert functions via protein-membrane interactions; however, the structural basis for such interactions has not been studied, and the nature of plant-specific insert-mediated membrane disruption has not been characterized. In the present study, the crystal structure of the saposin-like domain of potato aspartic protease was resolved at a resolution of 1.9 Å, revealing an open V-shaped configuration similar to the open structure of human saposin C. Notably, vesicle disruption activity followed Michaelis-Menten-like kinetics, a finding not previously reported for saposin-like proteins including plant-specific inserts. Circular dichroism data suggested that secondary structure was pH-dependent in a fashion similar to influenza A hemagglutinin fusion peptide. Membrane effects characterized by atomic force microscopy and light scattering indicated bilayer solubilization as well as fusogenic activity. Taken together, the present study is the first report to elucidate the membrane interaction mechanism of plant saposin-like domains whereby pH-dependent membrane interactions resulted in bilayer fusogenic activity that probably arose from a viral type pH-dependent helix-kink-helix motif at the plant-specific insert N terminus.
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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.