ArticleProceedings of the National Academy of Sciences of the United States of America2021
Myristoylation alone is sufficient for PKA catalytic subunits to associate with the plasma membrane to regulate neuronal functions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Mussel Spermatozoa Express a Specific Isoform of the Catalytic Subunit of cAMP-Dependent Protein Kinase.Molecular reproduction and development · 2026Article
- Crustacean Protein Kinases A and C: Bioinformatic Characterization in Decapods and Other Non-Model Organisms.International journal of molecular sciences · 2025Article
- The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- PKA regulation of neuronal function requires the dissociation of catalytic subunits from regulatory subunits.bioRxiv : the preprint server for biology · 2024Article
- Protein lipidation in health and disease: molecular basis, physiological function and pathological implication.Signal transduction and targeted therapy · 2024Review
- Review
- The putative myristoylome of Physcomitrium patens reveals conserved features of myristoylation in basal land plants.Plant cell reports · 2023Article
- Cell biology of protein-lipid conjugation.Cell structure and function · 2023Review
- Evolutionary and cellular analysis of the 'dark' pseudokinase PSKH2.The Biochemical journal · 2023Article
- Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023Article
- Protein acylation: mechanisms, biological functions and therapeutic targets.Signal transduction and targeted therapy · 2022Review
- Breadth and Specificity in Pleiotropic Protein Kinase A Activity and Environmental Responses.Frontiers in cell and developmental biology · 2022Review
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Myristoylation is a posttranslational modification that plays diverse functional roles in many protein species. The myristate moiety is considered insufficient for protein-membrane associations unless additional membrane-affinity motifs, such as a stretch of positively charged residues, are present. Here, we report that the electrically neutral N-terminal fragment of the protein kinase A catalytic subunit (PKA-C), in which myristoylation is the only functional motif, is sufficient for membrane association. This myristoylation can associate a fraction of PKA-C molecules or fluorescent proteins (FPs) to the plasma membrane in neuronal dendrites. The net neutral charge of the PKA-C N terminus is evolutionally conserved, even though its membrane affinity can be readily tuned by changing charges near the myristoylation site. The observed membrane association, while moderate, is sufficient to concentrate PKA activity at the membrane by nearly 20-fold and is required for PKA regulation of AMPA receptors at neuronal synapses. Our results indicate that myristoylation may be sufficient to drive functionally significant membrane association in the absence of canonical assisting motifs. This provides a revised conceptual base for the understanding of how myristoylation regulates protein functions.
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