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The protein encoded by MARCKS is a substrate for protein kinase C.
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Conditional deletion of MARCKS in ECs induces intracellular accumulation of mucins, elevated oxidative stress, and lipid droplet buildup.
MARCKS acts as a "molecular switch," binding to and regulating PIP2 signaling to regulate processes like proplatelet extension (microtubule-driven) vs proplatelet branching (Arp2/3 and actin polymerization-driven).
MARCKS knockdown arrested VSMC cell cycle by decreasing KIS (show UHMK1 ELISA Kits) expression. Decreased KIS (show UHMK1 ELISA Kits) expression resulted in nuclear trapping of p27kip1 (show CDKN1B ELISA Kits) in VSMCs.
MARCKS regulates the expression of proinflammatory cytokines in macrophages through activation of p38 (show CRK ELISA Kits)/JNK (show MAPK8 ELISA Kits) MAPK (show MAPK1 ELISA Kits) and NF-kappaB (show NFKB1 ELISA Kits).
Targeting phospho-MARCKS overcomes drug-resistance and induces antitumor activity in preclinical models of multiple myeloma.
Grin 1 is identified as a novel Cdk5 (show CDK5 ELISA Kits) substrate and MARCKS is confirmed as a Cdk5 (show CDK5 ELISA Kits) substrate.
MARCKS appears to be a nonessential regulatory protein in mast cell exocytosis but exerts a negative modulation.
MARCKS overexpression in the hippocampus of old mice leads to long-term potentiation and improved memory.
an important functional role for the interaction between MARCKS and PSA in the developing and adult nervous system.
cathepsin K (show CTSK ELISA Kits) exocytosis is controlled by PKCdelta (show PKCd ELISA Kits) through modulation of the actin bundling protein myristoylated alanine-rich C-kinase substrate.
Knockdown of MARCKS in HepG2 cells reduced cell migration and invasion, but not cell proliferation.
MARCKS upregulation increases vascular smooth muscle cell motility by activation of Rac1 and Cdc42 (show CDC42 ELISA Kits), promoting neointima formation.
A novel role for MARCKS in regulating nuclear functions such as gene expression.
unresponsiveness of breast cancer to paclitaxel treatment is, at least in part, mediated by phospho-MARCKS
MARCKS and PPP1R9A (show PPP1R9A ELISA Kits) might contribute to spine loss in schizophrenia and bipolar disorder through their interactions.
isotype delta-PKC is responsible for myristoylated alanine-rich C-kinase substrate (MARCKS) phosphorylation in human neutrophils following f-Met-Leu-Phe stimulation and MARCKS phosphorylation is essential for neutrophil migration and adhesion.
A key role of the effector domain of MARCKS in terms of cellular response, particularly to radiation: the importance of MARCKS phosphorylation status for its subcellular localization in lung cancer.
MARCKS overexpression was observed in several drug-resistant human myeloma cell lines and in drug-resistant primary multiple myeloma samples.
Finding that MARCKS acts as a mediator of apoptosis in microsatellite stable colorectal cancer cells adds a novel tumor-suppressing function to the established roles of MARCKS in cell motility and proliferation.
The protein encoded by this gene is a substrate for protein kinase C. It is localized to the plasma membrane and is an actin filament crosslinking protein. Phosphorylation by protein kinase C or binding to calcium-calmodulin inhibits its association with actin and with the plasma membrane, leading to its presence in the cytoplasm. The protein is thought to be involved in cell motility, phagocytosis, membrane trafficking and mitogenesis.
myristoylated alanine-rich C-kinase substrate
, myristoylated alanine-rich protein kinase C substrate (MARCKS, 80K-L)
, protein kinase C substrate, 80 kDa protein, light chain