ArticleScientific reports2016
Structural basis for the membrane association of ankyrinG via palmitoylation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Palmitoylation controls the stability of 190 kDa ankyrin-G in dendritic spines and is regulated by ZDHHC8 and lithium.Frontiers in molecular neuroscience · 2023Article
- Roles and mechanisms of ankyrin-G in neuropsychiatric disorders.Experimental & molecular medicine · 2022Review
- Dual ankyrinG and subpial autoantibodies in a man with well-controlled HIV infection with steroid-responsive meningoencephalitis: A case report.Frontiers in neurology · 2022Article
- Computational Study on the Function of Palmitoylation on the Envelope Protein in SARS-CoV-2.Journal of chemical theory and computation · 2021Article
- Roles of palmitoylation in structural long-term synaptic plasticity.Molecular brain · 2021Review
- Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii.Nature communications · 2019Article
- Coronavirus envelope protein: current knowledge.Virology journal · 2019Review
- Interplay between Membrane Curvature and Cholesterol: Role of Palmitoylated Caveolin-1.Biophysical journal · 2019Article
- Palmitoylated SCP1 is targeted to the plasma membrane and negatively regulates angiogenesis.eLife · 2017Article
- Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By clustering various ion channels and transporters, ankyrin-G (AnkG) configures the membrane-excitation platforms in neurons and cardiomyocytes. AnkG itself localizes to specific areas on the plasma membrane via s-palmitoylation of Cys. However, the structural mechanism by which AnkG anchors to the membrane is not understood. In this study, we solved the crystal structures of the reduced and oxidized forms of the AnkG s-palmitoylation domain and used multiple long-term coarse-grained molecular dynamics simulations to analyze their membrane association. Here we report that the membrane anchoring of AnkG was facilitated by s-palmitoylation, defining a stable binding interface on the lipid membrane, and that AnkG without s-palmitoylation also preferred to stay near the membrane but did not have a unique binding interface. This suggests that AnkG in the juxtamembrane region is primed to accept lipid modification at Cys, and once that happens AnkG constitutes a rigid structural base upon which a membrane-excitation platform can be assembled.
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