ArticleProceedings of the National Academy of Sciences of the United States of America2006
Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 99 citations in OpenAlex.
- Retroviruses and Cancer: Coevolution and Genetic Exchanges Between the Viral and the Host Genomes.Biology · 2026Article
- TOE1 is a β-catenin interacting protein regulating the proliferation of hematopoietic cells through PAK2 modulation.Stem cell reports · 2026Article
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- Multiomics analysis identifies oxidative phosphorylation as a cancer vulnerability arising from myristoylation inhibition.Journal of translational medicine · 2024Article
- Location, location, location: Protein kinase nanoclustering for optimised signalling output.eLife · 2024Review
- Cell biology of protein-lipid conjugation.Cell structure and function · 2023Review
- Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023Article
- Dual Role of ACBD6 in the Acylation Remodeling of Lipids and Proteins.Biomolecules · 2022Article
- Insights into the post-translational modification and its emerging role in shaping the tumor microenvironment.Signal transduction and targeted therapy · 2021Review
- Group I p21-activated kinases in leukemia cell adhesion to fibronectin.Cell adhesion & migration · 2021Article
- Post-translational Modifications of the Protein Termini.Frontiers in cell and developmental biology · 2021Review
- Curcumin Reduced HFrontiers in aging neuroscience · 2021Article
- Targeting N-myristoylation for therapy of B-cell lymphomas.Nature communications · 2020Article
- p21-Activated Kinases in Thyroid Cancer.Endocrinology · 2020Review
- PET Radiopharmaceuticals for Imaging Chemotherapy-Induced Cardiotoxicity.Current cardiology reports · 2020Review
- PAK1, PAK1Δ15, and PAK2: similarities, differences and mutual interactions.Scientific reports · 2019Article
- BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability.Experimental eye research · 2019Article
- 68Ga-Galmydar: A PET imaging tracer for noninvasive detection of Doxorubicin-induced cardiotoxicity.PloS one · 2019Article
- Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern.Nature chemical biology · 2018Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p21-activated protein kinase (PAK) 2 is a small GTPase-activated serine/threonine kinase regulating various cytoskeletal functions and is cleaved by caspase-3 during apoptosis. We demonstrate that the caspase-cleaved PAK2 C-terminal kinase fragment (C-t-PAK2) is posttranslationally myristoylated, although myristoylation is typically a cotranslational process. Myristoylation and an adjacent polybasic domain of C-t-PAK2 are sufficient to redirect EGFP from the cytosol to membrane ruffles and internal membranes. Membrane localization and the ability of C-t-PAK2 to induce cell death are significantly reduced when myristoylation is abolished. In addition, the proper myristoylation-dependent membrane localization of C-t-PAK2 significantly increased signaling through the stress-activated c-Jun N-terminal kinase signaling pathway, which often regulates apoptosis. Interestingly, C-t-PAK2 promoted cell death without compromising mitochondrial integrity. Posttranslational myristoylation of caspase-cleaved proteins involved in cytoskeletal dynamics (e.g., PAK2, actin, and gelsolin) might be part of a unique series of mechanisms involved in the regulation of the later events of apoptosis.
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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.