ReviewThe Biochemical journal2002
Cross-talk unfolded: MARCKS proteins.
Review in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
148 citing papers in PubMed, 302 citations in OpenAlex.
- Validation study of MARCKSL1 as a prognostic factor in lymph node-negative breast cancer patients.PloS one · 2019Trial
- Actin Cytoskeleton Dysregulation Links Testicular and Sperm Dysfunction in Type 1 Diabetes.International journal of molecular sciences · 2026Article
- Intrinsic Disorder and Phase Separation Coordinate Exocytosis, Motility, and Chromatin Remodeling in the Human Acrosomal Proteome.Proteomes · 2025Article
- MARCKS protein is a potential target in a naturally occurring equine model of neutrophilic asthma.Respiratory research · 2025Article
- Epigenetic and biogenetic regulation by polyphenols in prostate cancer in the context of 3P medicine.The EPMA journal · 2025Review
- CaScience advances · 2025Article
- Marcks overexpression in retinal ganglion cells promotes optic nerve regeneration.Cell death & disease · 2024Article
- Role for the PIPJournal of cell communication and signaling · 2024Review
- MARCKS Inhibition Alters Bovine Neutrophil Responses toBiomedicines · 2024Article
- MARCKS and PI(4,5)PMolecular biology of the cell · 2024Article
- A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in βCell adhesion & migration · 2023Article
- Review
- Clinical relevance of biomarkers, new therapeutic approaches, and role of post-translational modifications in the pathogenesis of Alzheimer's disease.Frontiers in aging neuroscience · 2022Review
- Pathophysiological roles of myristoylated alanine-rich C-kinase substrate (MARCKS) in hematological malignancies.Biomarker research · 2021Review
- Proteomic analysis of urinary and tissue-exudative extracellular vesicles to discover novel bladder cancer biomarkers.Cancer science · 2021Article
- A cell-penetrating MARCKS mimetic selectively triggers cytolytic death in glioblastoma.Oncogene · 2020Article
- MARCKS mediates vascular contractility through regulating interactions between voltage-gated CaVascular pharmacology · 2020Article
- A polybasic domain in aPKC mediates Par6-dependent control of membrane targeting and kinase activity.The Journal of cell biology · 2020Article
- MARCKSL1 promotes the proliferation, migration and invasion of lung adenocarcinoma cells.Oncology letters · 2020Article
- YAP-dependent necrosis occurs in early stages of Alzheimer's disease and regulates mouse model pathology.Nature communications · 2020Article
88 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteins of the MARCKS (myristoylated alanine-rich C kinase substrate) family were first identified as prominent substrates of protein kinase C (PKC). Since then, these proteins have been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and neurosecretion. The effector domain of MARCKS proteins is phosphorylated by PKC, binds to calmodulin and contributes to membrane binding. This multitude of mutually exclusive interactions allows cross-talk between the signal transduction pathways involving PKC and calmodulin. This review focuses on recent, mostly biophysical and biochemical results renewing interest in this protein family. MARCKS membrane binding is now understood at the molecular level. From a structural point of view, there is a consensus emerging that MARCKS proteins are "natively unfolded". Interestingly, domains similar to the effector domain have been discovered in other proteins. Furthermore, since the effector domain enhances the polymerization of actin in vitro, MARCKS proteins have been proposed to mediate regulation of the actin cytoskeleton. However, the recent observations that MARCKS might serve to sequester phosphatidylinositol 4,5-bisphosphate in the plasma membrane of unstimulated cells suggest an alternative model for the control of the actin cytoskeleton. While myristoylation is classically considered to be a co-translational, irreversible event, new reports on MARCKS proteins suggest a more dynamic picture of this protein modification. Finally, studies with mice lacking MARCKS proteins have investigated the functions of these proteins during embryonic development in the intact organism.
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What OpenQuestion holds
Registered trials
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.