ArticleMolecular biology of the cell2014
Interplay between phosphorylation and palmitoylation mediates plasma membrane targeting and sorting of GAP43.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Protein palmitoylation is involved in regulating mouse sperm motility via the signals of calcium, protein tyrosine phosphorylation and reactive oxygen species.Biological research · 2025Article
- Phosphorylation on serine 72 modulates Rab7A palmitoylation and retromer recruitment.Journal of cell science · 2025Article
- Emerging strategies for treating autoimmune disease with genetically modified dendritic cells.Cell communication and signaling : CCS · 2024Review
- Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications.The Journal of cell biology · 2023Article
- Article
- Control of a hippocampal recurrent excitatory circuit by cannabinoid receptor-interacting protein Gap43.Nature communications · 2023Article
- S-Palmitoylation of Synaptic Proteins in Neuronal Plasticity in Normal and Pathological Brains.Cells · 2023Review
- Lost in traffic: consequences of altered palmitoylation in neurodegeneration.Frontiers in physiology · 2023Review
- Coordinated interplay between palmitoylation, phosphorylation and SUMOylation regulates kainate receptor surface expression.Frontiers in molecular neuroscience · 2023Article
- Review
- Generation of a Retina Reporter hiPSC Line to Label Progenitor, Ganglion, and Photoreceptor Cell Types.Translational vision science & technology · 2020Article
- GAP-43 and BASP1 in Axon Regeneration: Implications for the Treatment of Neurodegenerative Diseases.Frontiers in cell and developmental biology · 2020Review
- Zdhhc2 Is Essential for Plasmacytoid Dendritic Cells Mediated Inflammatory Response in Psoriasis.Frontiers in immunology · 2020Article
- Stress-induced Changes in the S-palmitoylation and S-nitrosylation of Synaptic Proteins.Molecular & cellular proteomics : MCP · 2019Article
- Network Analysis of a Membrane-Enriched Brain Proteome across Stages of Alzheimer's Disease.Proteomes · 2019Article
- The Interactome of Palmitoyl-Protein Thioesterase 1 (PPT1) Affects Neuronal Morphology and Function.Frontiers in cellular neuroscience · 2019Article
- Global, site-specific analysis of neuronal protein S-acylation.Scientific reports · 2017Article
- A Shift from a Pivotal to Supporting Role for the Growth-Associated Protein (GAP-43) in the Coordination of Axonal Structural and Functional Plasticity.Frontiers in cellular neuroscience · 2017Review
- The Networks of Genes Encoding Palmitoylated Proteins in Axonal and Synaptic Compartments Are Affected in PPT1 Overexpressing Neuronal-Like Cells.Frontiers in molecular neuroscience · 2017Article
- Regulation of TRPP3 Channel Function by N-terminal Domain Palmitoylation and Phosphorylation.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation and lipidation provide posttranslational mechanisms that contribute to the distribution of cytosolic proteins in growing nerve cells. The growth-associated protein GAP43 is susceptible to both phosphorylation and S-palmitoylation and is enriched in the tips of extending neurites. However, how phosphorylation and lipidation interplay to mediate sorting of GAP43 is unclear. Using a combination of biochemical, genetic, and imaging approaches, we show that palmitoylation is required for membrane association and that phosphorylation at Ser-41 directs palmitoylated GAP43 to the plasma membrane. Plasma membrane association decreased the diffusion constant fourfold in neuritic shafts. Sorting to the neuritic tip required palmitoylation and active transport and was increased by phosphorylation-mediated plasma membrane interaction. Vesicle tracking revealed transient association of a fraction of GAP43 with exocytic vesicles and motion at a fast axonal transport rate. Simulations confirmed that a combination of diffusion, dynamic plasma membrane interaction and active transport of a small fraction of GAP43 suffices for efficient sorting to growth cones. Our data demonstrate a complex interplay between phosphorylation and lipidation in mediating the localization of GAP43 in neuronal cells. Palmitoylation tags GAP43 for global sorting by piggybacking on exocytic vesicles, whereas phosphorylation locally regulates protein mobility and plasma membrane targeting of palmitoylated GAP43.
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