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MARCKSL1 encodes a member of the myristoylated alanine-rich C-kinase substrate (MARCKS) family.
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MARCKSL1 showed potent anti-angiogenic activity and reduced the levels of VEGF (zeige VEGFA Proteine) and HIF-1alpha (zeige HIF1A Proteine) expression. MARCKSL1 decreased VEGFinduced phosphorylation of the PI3K (zeige PIK3CA Proteine)/Akt (zeige AKT1 Proteine) signaling pathway components.
MARCKSL1 suppresses LOXL2 (zeige LOXL2 Proteine)-induced oncogenesis.
Patients with high expression of PPH3 (zeige PPP4C Proteine) and high MARCKSL1 protein had a lower survival rate versus patients with low MARCKSL1 and high PPH3 (zeige PPP4C Proteine) expression.
Gene knockdown in prostate cancer cells or in neurons reveals a critical role for MARCKSL1 in migration that is dependent on the phosphorylation state.
We suggest that the downregulation of MRP by beta3 is not required for increased cell spreading but instead that MRP downregulation is a secondary effect of increased cell spreading.
Mutation analysis of MLP demonstrated that myristoylation was necessary to promote proliferation and that phosphorylation inhibited proliferation, indicating the functional importance of membrane localization
This gene encodes a member of the myristoylated alanine-rich C-kinase substrate (MARCKS) family. Members of this family play a role in cytoskeletal regulation, protein kinase C signaling and calmodulin signaling. The encoded protein affects the formation of adherens junction. Alternative splicing results in multiple transcript variants. Pseudogenes of this gene are located on the long arm of chromosomes 6 and 10.
, MARCKS-related protein
, MARCKS-like protein 1
, macrophage myristoylated alanine-rich C kinase substrate
, brain protein F52
, myristoylated alanine-rich C kinase substrate