ArticleMolecular pharmacology2015
Protein Kinase C (PKC)ζ Pseudosubstrate Inhibitor Peptide Promiscuously Binds PKC Family Isoforms and Disrupts Conventional PKC Targeting and Translocation.
Article in Molecular pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
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- Gastrointestinal Permeation Enhancers Beyond Sodium Caprate and SNAC - What is Coming Next?Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Genetic mechanisms for impaired synaptic plasticity in schizophrenia revealed by computational modeling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Emerging molecular therapies in the treatment of bladder cancer.Exploration of targeted anti-tumor therapy · 2024Review
- Storming the gate: New approaches for targeting the dynamic tight junction for improved drug delivery.Advanced drug delivery reviews · 2023Review
- Candidate Genes and Gene Networks Change with Age in Japanese Black Cattle by Blood Transcriptome Analysis.Genes · 2023Article
- Impact of peptide permeation enhancer on tight junctions opening cellular mechanisms.Biochemistry and biophysics reports · 2022Article
- A novel non‑selective atypical PKC agonist could protect neuronal cell line from Aβ‑oligomer induced toxicity by suppressing Aβ generation.Molecular medicine reports · 2022Article
- Involvement of PKMζ in Stress Response and Depression.Frontiers in cellular neuroscience · 2022Review
- Activators and Inhibitors of Protein Kinase C (PKC): Their Applications in Clinical Trials.Pharmaceutics · 2021Review
- Desmin aggrephagy in rat and human ischemic heart failure through PKCζ and GSK3β as upstream signaling pathways.Cell death discovery · 2021Article
- Memory Destabilization and Reconsolidation Dynamically Regulate the PKMζ Maintenance Mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- p53 destabilizing protein skews asymmetric division and enhances NOTCH activation to direct self-renewal of TICs.Nature communications · 2020Article
- Scabronine G Methyl Ester Improves Memory-Related Behavior and Enhances Hippocampal Cell Proliferation and Long-Term Potentiation via the BDNF-CREB Pathway in Olfactory Bulbectomized Mice.Frontiers in pharmacology · 2020Article
- Reversing Cocaine-Induced Plasticity with Zeta Inhibitory Peptide.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Protein Kinase C: Targets to Regenerate Brain Injuries?Frontiers in cell and developmental biology · 2019Article
- aPKC controls endothelial growth by modulating c-Myc via FoxO1 DNA-binding ability.Nature communications · 2018Article
- Actin polymerization controls cilia-mediated signaling.The Journal of cell biology · 2018Article
- Evolving mechanisms of vascular smooth muscle contraction highlight key targets in vascular disease.Biochemical pharmacology · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
PKMζ is generated via an alternative transcriptional start site in the atypical protein kinase C (PKC)ζ isoform, which removes N-terminal regulatory elements, including the inhibitory pseudosubstrate domain, consequently rendering the kinase constitutively active. Persistent PKMζ activity has been proposed as a molecular mechanism for the long-term maintenance of synaptic plasticity underlying some forms of memory. Many studies supporting a role for PKMζ in synaptic plasticity and memory have relied on the PKCζ pseudosubstrate-derived ζ-inhibitory peptide (ZIP). However, recent studies have demonstrated that ZIP-induced impairments to synaptic plasticity and memory occur even in the absence of PKCζ, suggesting that ZIP exerts its actions via additional cellular targets. In this study, we demonstrated that ZIP interacts with conventional and novel PKC, in addition to atypical PKC isoforms. Moreover, when brain abundance of each PKC isoform and affinity for ZIP are taken into account, the signaling capacity of ZIP-responsive pools of conventional and novel PKCs may match or exceed that for atypical PKCs. Pseudosubstrate-derived peptides, like ZIP, are thought to exert their cellular action primarily by inhibiting PKC catalytic activity; however, the ZIP-sensitive catalytic core of PKC is known to participate in the enzyme's subcellular targeting, suggesting an additional mode of ZIP action. Indeed, we have demonstrated that ZIP potently disrupts PKCα interaction with the PKC-targeting protein A-kinase anchoring protein (AKAP) 79 and interferes with ionomycin-induced translocation of conventional PKC to the plasma membrane. Thus, ZIP exhibits broad-spectrum action toward the PKC family of enzymes, and this action may contribute to its unique ability to impair memory.
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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.