{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMARCKS is a major substrate of protein kinase C that underpins a variety of basic cellular functions through dynamic regulation of the actin cytoskeleton and plasma membrane lipids. Upon phosphorylation, MARCKS releases its bound phosphatidylinositol 4,5‐bisphosphate (PIP2) and translocates from the membrane to the cytosol, thereby orchestrating the assembly of signaling complexes that drive processes such as neurite initiation, myoblast fusion, cytokinesis, and regulated secretion. In addition, MARCKS interacts with calmodulin and specific intracellular chaperones and—even translocating to the nucleus via a sequence within its effector domain—it may influence gene expression and cell‐cycle progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAberrant expression and phosphorylation of MARCKS have been implicated in a wide range of human malignancies where the protein drives tumor progression by enhancing cell migration, invasion, and resistance to apoptosis. For example, in prostate cancer MARCKS is a target of oncogenic microRNAs that promote an invasive phenotype, while in glioblastoma and multiple myeloma MARCKS activity potentiates pathways such as AKT/mTOR or functions as an E2F‐1 cofactor to expedite cell‐cycle progression. Likewise, in cholangiocarcinoma, colorectal, breast, and kidney cancers, dysregulated MARCKS signaling modulates receptor‐activated cascades, affects exosome content and cancer–associated fibroblast activation, and ultimately contributes to angiogenesis and metastasis. The emerging data indicate that targeted inhibition of MARCKS or its phosphorylation may restore drug sensitivity and curb tumor aggressiveness."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in cancer, MARCKS is critical for numerous physiological processes. The protein regulates immune cell migration and adhesion—as observed in neutrophils and B lymphocytes—contributes to synaptic plasticity and the maintenance of dendritic spines (implicated in conditions such as Alzheimer’s disease and schizophrenia) and governs mucin secretion by airway epithelial cells. MARCKS also modulates endothelial responses to vasoactive agents and participates in intracellular signaling cascades that impact vascular smooth muscle behavior and hepatic stellate cell activation. These multifaceted functions mark MARCKS as a pivotal node in both normal cell physiology and disease, and they underscore the promise of MARCKS‐targeted strategies for therapeutic intervention."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Michelle E Rauch, Colin G Ferguson, Glenn D Prestwich, et al. 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