A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β2-integrin activation and signaling

Cell Adh Migr. 2023 Dec;17(1):1-16. doi: 10.1080/19336918.2023.2233204.


MARCKS is an actin and PIP2-binding protein that plays an essential role in neutrophil migration and adhesion; however, the molecular details regarding MARCKS function in these processes remains unclear. Neutrophil adhesion and migration also require the cell surface receptors β2-integrins. We hypothesized that MARCKS inhibition would alter neutrophil β2-integrin activation and signaling. We utilized a MARCKS-targeting peptide to inhibit MARCKS in inside-out and outside-in β2-integrin activation in neutrophils. MANS-mediated MARCKS inhibition had no significant effect on inside-out β2-integrin activation. MANS treatment significantly attenuated ICAM-1/Mn2+-stimulated static adhesion, cell spreading and β2-integrin clustering, suggesting a role for MARCKS function in outside-in β2-integrin activation. Additional work is needed to better understand the molecular mechanisms of MARCKS role in outside-in β2-integrin activation and signaling.

Keywords: Beta2-integrin; ICAM-1; MARCKS; neutrophils; outside-in.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine
  • CD18 Antigens* / metabolism
  • Myristoylated Alanine-Rich C Kinase Substrate* / antagonists & inhibitors
  • Neutrophils*
  • Peptides / pharmacology
  • Signal Transduction


  • Alanine
  • CD18 Antigens
  • Peptides
  • Myristoylated Alanine-Rich C Kinase Substrate