ArticleeLife2017
Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane.
Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2025Review
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- PI(4,5)P2: signaling the plasma membrane.The Biochemical journal · 2022Article
- The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE-SNARE interactions.eLife · 2021Article
- Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity.Nature communications · 2021Article
- The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation.The Journal of biological chemistry · 2020Article
- PtdIns4P-mediated electrostatic forces influence S-acylation of peripheral proteins at the Golgi complex.Bioscience reports · 2020Article
- Acid Sphingomyelinase regulates the localization and trafficking of palmitoylated proteins.Biology open · 2019Article
- The cysteine-rich domain of synaptosomal-associated protein of 23 kDa (SNAP-23) regulates its membrane association and regulated exocytosis from mast cells.Biochimica et biophysica acta. Molecular cell research · 2019Article
- Article
- Differential organization of tonic and chronic B cell antigen receptors in the plasma membrane.Nature communications · 2019Article
- Review
- t-SNARE Transmembrane Domain Clustering Modulates Lipid Organization and Membrane Curvature.Journal of the American Chemical Society · 2017Article
- Membrane targeting of inhibitory Smads through palmitoylation controls TGF-β/BMP signaling.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Rab5 is critical for SNAP23 regulated granule-granule fusion during compound exocytosis.Scientific reports · 2017Article
- Structural Basis for Substrate Recognition by the Ankyrin Repeat Domain of Human DHHC17 Palmitoyltransferase.Structure (London, England : 1993) · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SNAREs SNAP25 and SNAP23 are proteins that are initially cytosolic after translation, but then become stably attached to the cell membrane through palmitoylation of cysteine residues. For palmitoylation to occur, membrane association is a prerequisite, but it is unclear which motif may increase the affinities of the proteins for the target membrane. In experiments with rat neuroendocrine cells, we find that a few basic amino acids in the cysteine-rich region of SNAP25 and SNAP23 are essential for plasma membrane targeting. Reconstitution of membrane-protein binding in a liposome assay shows that the mechanism involves protein electrostatics between basic amino acid residues and acidic lipids such as phosphoinositides that play a primary role in these interactions. Hence, we identify an electrostatic anchoring mechanism underlying initial plasma membrane contact by SNARE proteins, which subsequently become palmitoylated at the plasma membrane.
Indexed as
Identifiers
What OpenQuestion holds
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.