Myristoylated alanine-rich C-kinase substrate effector domain phosphorylation regulates the growth and radiation sensitization of glioblastoma.

ABSTRACT: Glioblastoma harbors frequent alterations in receptor tyrosine kinases, phosphatidylinositol‑3 kinase (PI3K) and phosphatase and tensin homolog (PTEN) that dysregulate phospholipid signaling driven tumor proliferation and therapeutic resistance. Myristoylated alanine‑rich C‑kinase substrate (MARCKS) is a 32 kDa intrinsically unstructured protein containing a polybasic (+13) effector domain (ED), which regulates its electrostatic sequestration of phospholipid phosphatidylinositol (4,5)‑bisphosphate (PIP2), and its binding to phosphatidylserine, calcium/calmodulin, filamentous actin, while also serving as a nuclear localization sequence. MARCKS ED is phosphorylated by protein kinase C (PKC) and Rho‑associated protein kinase (ROCK) kinases; however, the impact of MARCKS on glioblastoma growth

SUBMITTER: Eustace NJ 

PROVIDER: S-EPMC6521926 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature