ArticleJournal of cell science2011
Differential palmitoylation regulates intracellular patterning of SNAP25.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 59 citations in OpenAlex.
- Steric confinement-induced emission probe for monitoring protein conformations in live cells.Communications chemistry · 2026Article
- Palmitoylation Code and Endosomal Sorting Regulate ABHD17A Plasma Membrane Targeting and Activity.International journal of molecular sciences · 2025Article
- Recent advances in S-palmitoylation and its emerging roles in human diseases.Journal of hematology & oncology · 2025Review
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- Palmitoylation of synaptic proteins: roles in functional regulation and pathogenesis of neurodegenerative diseases.Cellular & molecular biology letters · 2024Review
- Regulation of cardiomyocyte intracellular trafficking and signal transduction by protein palmitoylation.Biochemical Society transactions · 2024Article
- OnabotulinumtoxinA effects on trigeminal nociceptors.Cephalalgia : an international journal of headache · 2023Article
- Palmitoylation of Voltage-Gated Ion Channels.International journal of molecular sciences · 2022Review
- Graph-theoretic constraints on vesicle traffic networks.Journal of biosciences · 2022Article
- Regulation of hippocampal excitatory synapses by the Zdhhc5 palmitoyl acyltransferase.Journal of cell science · 2021Article
- Regulatory effects of protein S-acylation on insulin secretion and insulin action.Open biology · 2021Review
- A peptidic inhibitor for PD-1 palmitoylation targets its expression and functions.RSC chemical biology · 2021Article
- Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021Review
- 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
- 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
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- The C-terminal domain of zDHHC2 contains distinct sorting signals that regulate intracellular localisation in neurons and neuroendocrine cells.Molecular and cellular neurosciences · 2017Article
- Phosphorylation of SNAP-23 regulates its dynamic membrane association during mast cell exocytosis.Biology open · 2017Article
- Global, site-specific analysis of neuronal protein S-acylation.Scientific reports · 2017Article
- Protein Palmitoylation and Its Role in Bacterial and Viral Infections.Frontiers in immunology · 2017Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
SNAP25 regulates membrane fusion events at the plasma membrane and in the endosomal system, and a functional pool of the protein is delivered to recycling endosomes (REs) and the trans Golgi network (TGN) through an ARF6-dependent cycling pathway. SNAP25 is a peripheral membrane protein, and palmitoylation of a cluster of four cysteine residues mediates its stable association with the membrane. Here, we report that palmitoylation also determines the precise intracellular distribution of SNAP25, and that mutating single palmitoylation sites enhances the amount of SNAP25 at the RE and TGN. The farnesylated CAAX motif from Hras was ligated onto a SNAP25 mutant truncated immediately distal to the cysteine-rich domain. This construct displayed the same intracellular distribution as full-length SNAP25, and decreasing the number of cysteine residues in this construct increased its association with the RE and TGN, confirming the dominant role of the cysteine-rich domain in directing the intracellular distribution of SNAP25. Marked differences in the localisations of SNAP25-CAAX and Hras constructs, each with two palmitoylation sites, were observed, showing that subtle differences in palmitoylated sequences can have a major impact upon intracellular targeting. We propose that the cysteine-rich domain of SNAP25 is designed to facilitate the dual function of this SNARE protein at the plasma membrane and endosomes, and that dynamic palmitoylation acts as a mechanism to regulate the precise intracellular patterning of SNAP25.
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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.