anti-Myristoylated Alanine-Rich Protein Kinase C Substrate (MARCKS) Antibodies

Xenopus laevis Myristoylated Alanine-Rich Protein Kinase C Substrate (MARCKS) interaction partners

1. 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.

Mouse (Murine) Myristoylated Alanine-Rich Protein Kinase C Substrate (MARCKS) interaction partners

1. While the presence of MARCKS does not affect whole brain levels of activated or total CDC42, authors propose that MARCKS is uniquely positioned to regulate CDC42 localization and interactions within specialized cellular compartments, such as nascent neurites.

2. Study in mice reports that Marcks is regulated by acetylation through Tip60 and Sirt2. Maternal diabetes-induced MARCKS acetylation is required for its phosphorylation, which disables the protective effects of MARCKS on mitochondria and the endoplasmic reticulum, leading to cellular organelle stress and neural tube defect formation.

3. this work establishes a novel role for MARCKS in axon dynamics and highlights the necessity of MARCKS as an organizer of DCC signaling at the membrane.

4. Strongly support the existence of a PKC-MARCKS-PI3K regulatory module.

5. ENaC activity is regulated by calpain-2 proteolysis of MARCKS.

6. In the absence of Pin1, MARCKS is hyper-phosphorylated, leading to loss of cell adhesions, and collapse of the growth cone.

7. Findings suggest that MIR429 modulates mucin secretion in human colorectal cells and mouse colitis tissues by up-regulating of MARCKS expression.

8. Conditional deletion of MARCKS in ECs induces intracellular accumulation of mucins, elevated oxidative stress, and lipid droplet buildup.

9. 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).

10. MARCKS knockdown arrested VSMC cell cycle by decreasing KIS expression. Decreased KIS expression resulted in nuclear trapping of p27kip1 in VSMCs.

11. MARCKS regulates the expression of proinflammatory cytokines in macrophages through activation of p38/JNK MAPK and NF-kappaB.

12. Targeting phospho-MARCKS overcomes drug-resistance and induces antitumor activity in preclinical models of multiple myeloma.

13. Grin 1 is identified as a novel Cdk5 substrate and MARCKS is confirmed as a Cdk5 substrate.

14. MARCKS appears to be a nonessential regulatory protein in mast cell exocytosis but exerts a negative modulation.

15. MARCKS overexpression in the hippocampus of old mice leads to long-term potentiation and improved memory.

16. an important functional role for the interaction between MARCKS and PSA in the developing and adult nervous system.

17. cathepsin K exocytosis is controlled by PKCdelta through modulation of the actin bundling protein myristoylated alanine-rich C-kinase substrate.

18. These results suggest that MARCKS is involved in directed migration of macrophages

19. 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.

20. the capacity of MARCKS-ED to regulate granule exocytosis in a PKC-dependent manner, consistent with regulated sequestration of phosphoinositides that mediate granule fusion at the plasma membrane.

Zebrafish Myristoylated Alanine-Rich Protein Kinase C Substrate (MARCKS) interaction partners

1. Marcksb is required for proper gastrulation movements of zebrafish.

Human Myristoylated Alanine-Rich Protein Kinase C Substrate (MARCKS) interaction partners

1. Study, using a tetracyclineinducible system in PTENnull U87 cells, demonstrated that MARCKS overexpression suppresses growth and enhances radiation sensitivity in vivo. The overexpression of the nonphosphorylatable effector domain (ED) mutant exerted growthsuppressive and radiationsensitizing effects, while the pseudophosphorylated ED mutant exhibited an enhanced colony formation and clonogenic survival ability.

2. Study found that the expression of MARCKS was significantly upregulated in glioblastoma (GBM) and was associated with a poor clinical outcome in patients with GBM. Knockdown of MARCKS suppressed the migration and invasion of GBM cells in vitro and reduced the expression of phosphorylated phosphoinositide 3kinase and protein kinase B, as well as SNAI1 expression.

3. MARCKS is a putative target for drug design.

4. High MARCKS expression is associated with liver tumor.

5. Raman spectra show vibrational bands of Phenylalanine and Lysine residues specific for the protein effector domain, and evidence the presence of alpha helix structure in both configurations.

6. tromal MARCKS overexpression in tumors might contribute to cancer-associated fibroblasts activation and to the poor prognosis of Epithelial ovarian cancer.

7. Study identifies MARCKS phosphorylation at Ser46 is a hallmark of neurite degeneration, the classical hallmark of Alzheimer's disease (AD) pathology. MARCKS phosphorylation is induced by HMGB1 via TLR4.

8. 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.

9. MARCKS overexpression might in part explain the poor prognosis of inflammatory breast cancer.

10. 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.

11. Data indicate MARCKS (myristoylated alanine-rich C-kinase substrate) as a target of miR-21.

12. data suggest a major contribution of MARCKS to kidney cancer growth and provide an alternative therapeutic strategy of improving the efficacy of multikinase inhibitors.

13. These data suggested that miR34c3p acts as a tumor suppressor via regulation of MARCKS expression in OS progression

14. Ca(2+)-PKC-MARCKS-PIP2-PI3K-PIP3 system functions as an activation module in vitro

15. 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).

16. Findings suggest that MIR429 modulates mucin secretion in human colorectal cells and mouse colitis tissues by up-regulating of MARCKS expression.

17. Knockdown of MARCKS in HepG2 cells reduced cell migration and invasion, but not cell proliferation.

18. MARCKS upregulation increases vascular smooth muscle cell motility by activation of Rac1 and Cdc42, promoting neointima formation.

19. A novel role for MARCKS in regulating nuclear functions such as gene expression.

20. MARCKS knockdown arrested VSMC cell cycle by decreasing KIS expression. Decreased KIS expression resulted in nuclear trapping of p27kip1 in VSMCs.

Cow (Bovine) Myristoylated Alanine-Rich Protein Kinase C Substrate (MARCKS) interaction partners

1. MARCKS protein mediates hydrogen peroxide regulation of endothelial permeability.

2. 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.

3. These findings demonstrate a critical role for MARCKS-phosphatidylinositol-4,5-diphosphate signaling in regulating dendrite development.

4. Protein kinase C mediated inhibition of endothelial L-arginine transport is mediated by MARCKS protein