ArticleNature chemical biology2012
Transient GPI-anchored protein homodimers are units for raft organization and function.
Article in Nature chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.
What it found
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Who cites it
125 citing papers in PubMed, 269 citations in OpenAlex.
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- Action of the Terminal Complement Pathway on Cell Membranes.The Journal of membrane biology · 2025Review
- Extracellular vesicles adhere to cells primarily by interactions of integrins and GM1 with laminin.The Journal of cell biology · 2025Article
- Uptake of small extracellular vesicles by recipient cells is facilitated by paracrine adhesion signaling.Nature communications · 2025Article
- Biomembrane structure at the molecular level and its application in precision medicine.Biophysics reviews · 2025Review
- Unremodeled GPI-anchored proteins at the plasma membrane trigger aberrant endocytosis.Life science alliance · 2025Article
- Microenvironment-confined kinetic elucidation and implementation of a DNA nano-phage with a shielded internal computing layer.Nature communications · 2025Article
- Recent Advancements in Imaging Techniques for Individual Extracellular Vesicles.Molecules (Basel, Switzerland) · 2024Review
- Why nature evolved GPI-anchored proteins: unique structure characteristics enable versatile cell surface functions.Glycobiology · 2024Review
- A non-toxic equinatoxin-II reveals the dynamics and distribution of sphingomyelin in the cytosolic leaflet of the plasma membrane.Scientific reports · 2024Article
- Is cholesterol both the lock and key to abnormal transmembrane signals in Autism Spectrum Disorder?Lipids in health and disease · 2024Article
65 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Advanced single-molecule fluorescent imaging was applied to study the dynamic organization of raft-associated glycosylphosphatidylinositol-anchored proteins (GPI-APs) in the plasma membrane and their stimulation-induced changes. In resting cells, virtually all of the GPI-APs are mobile and continually form transient (~200 ms) homodimers (termed homodimer rafts) through ectodomain protein interactions, stabilized by the presence of the GPI-anchoring chain and cholesterol. Heterodimers do not form, suggesting a fundamental role for the specific ectodomain protein interaction. Under higher physiological expression conditions , homodimers coalesce to form hetero- and homo-GPI-AP oligomer rafts through raft-based lipid interactions. When CD59 was ligated, it formed stable oligomer rafts containing up to four CD59 molecules, which triggered intracellular Ca(2+) responses that were dependent on GPI anchorage and cholesterol, suggesting a key part played by transient homodimer rafts. Transient homodimer rafts are most likely one of the basic units for the organization and function of raft domains containing GPI-APs.
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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.