Myristoylated alanine-rich C-kinase substrate-like protein 1 (MARCKSL1)

Myristoylated alanine-rich C-kinase substrate-like protein 1 (MARCKSL1) is a member of the MARCKS protein family, encoded by the *MARCKSL1* gene. It is an actin-binding protein regulated by phosphorylation, prominently by protein kinase C (PKC) and JNK, modulating its localization between the plasma membrane and cytoplasm. MARCKSL1 organizes the actin cytoskeleton, controls filopodia and lamellipodia formation, and thereby regulates cell migration, proliferation, adhesion, and vesicle trafficking. Expressed highly in the nervous system and during development, MARCKSL1 is critical for neural tube closure and tissue regeneration. It is overexpressed in several cancers where it drives proliferation, invasion, migration, and epithelial-mesenchymal transition (EMT) through pathways including PI3K/AKT. High levels predict poor prognosis in certain cancers. Because of its multifaceted roles in both development and disease, MARCKSL1 is a candidate target in oncology and regenerative medicine, but broad physiological functions may present therapeutic safety challenges.

Other names

MARCKS-related proteinMLPMRPMacMARCKSF52MLP1MARCKS-like protein 1Macrophage myristoylated alanine-rich C kinase substratemac-MARCKSMACMARCKSBrain protein F52

Research suggests inhibition or knockdown of MARCKSL1 decreases proliferation and invasion of cancer cells—primarily via control of actin cytoskeleton and signal transduction.