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The protein encoded by MARCKS is a substrate for protein kinase C. Additionally we are shipping MARCKS Antibodies (245) and MARCKS Proteins (7) and many more products for this protein.
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The results indicated MARCKS may be the missing link in the regulation of the function (i.e., sodium transport) of epithelial sodium channels by anionic phospholipids.
ENaC (show SCNN1A ELISA Kits) activity is regulated by calpain-2 (show CAPN2 ELISA Kits) proteolysis of MARCKS.
In the absence of Pin1 (show PIN1 ELISA Kits), MARCKS is hyper-phosphorylated, leading to loss of cell adhesions, and collapse of the growth cone.
Findings suggest that MIR429 modulates mucin (show SLC13A2 ELISA Kits) secretion in human colorectal cells and mouse colitis tissues by up-regulating of MARCKS expression.
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 expression. Decreased KIS 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.
Marcksb is required for proper gastrulation movements of zebrafish.
we propose a role for MARCKS in a novel mechanism of BTZ resistance via exocytosis of ubiquitinated proteins in BTZ-resistant cells leading to quenching of proteolytic stress.
MARCKS overexpression might in part explain the poor prognosis of inflammatory breast cancer.
Authors determined that myristoylated alanine-rich C-kinase substrate (MARCKS) was highly expressed in ovarian stroma, and was required for the differentiation and tumor promoting function of CAFs (show TBX1 ELISA Kits).
Data indicate MARCKS (myristoylated alanine-rich C-kinase substrate) as a target of miR (show MLXIP ELISA Kits)-21.
data suggest a major contribution of MARCKS to kidney cancer growth and provide an alternative therapeutic strategy of improving the efficacy of multikinase inhibitors.
These data suggested that miR34c3p acts as a tumor suppressor via regulation of MARCKS expression in OS progression
Ca(2+)-PKC-MARCKS-PIP2-PI3K-PIP3 system functions as an activation module in vitro
Findings show that calmodulin (CaM) stimulates phosphoinositide-3-kinase (PI3K) lipid kinase activity by binding MARCKS and displacing it from phosphatidylinositol 4,5-bisphosphate (PIP2) headgroups, thereby releasing free PIP2 that recruits active PI3K to the membrane and serves as the substrate for the generation of phosphatidylinositol 3,4,5-trisphosphate (PIP3).
Knockdown of MARCKS in HepG2 cells reduced cell migration and invasion, but not cell proliferation.
MARCKS protein mediates hydrogen peroxide regulation of endothelial permeability.
a critical role for H(2)O(2) in angiotensin-II signaling to the endothelial cytoskeleton in a novel pathway that is critically dependent on MARCKS, Rac1, and c-Abl.
These findings demonstrate a critical role for MARCKS-phosphatidylinositol-4,5-diphosphate signaling in regulating dendrite development.
Protein kinase C (show PKC ELISA Kits) mediated inhibition of endothelial L-arginine (show GATM ELISA Kits) transport is mediated by MARCKS protein
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 protein kinase C substrate
, methyl binding domain
, myristoylated alanine-rich C-kinase substrate
, Myristoylated alanine-rich protein kinase C substrate
, protein kinase C substrate 80 kDa protein
, myristoylated alanine-rich protein kinase C substrate (MARCKS, 80K-L)
, protein kinase C substrate, 80 kDa protein, light chain
, myristoylated alanine-rich C kinase substrate (MARCKS)