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

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 β 2 -integrins. We hyp...

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Bibliographic Details
Published in:Cell adhesion & migration 2023-12, Vol.17 (1), p.1-16
Main Authors: Conley, Haleigh, Till, Rebecca L., Berglund, Alix K., Jones, Samuel L., Sheats, M. Katie
Format: Article
Language:English
Subjects:
Beta2-integrin
ICAM-1
MARCKS
neutrophils
outside-in
Research Paper
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Summary: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 β 2 -integrins. We hypothesized that MARCKS inhibition would alter neutrophil β 2 -integrin activation and signaling. We utilized a MARCKS-targeting peptide to inhibit MARCKS in inside-out and outside-in β 2 -integrin activation in neutrophils. MANS-mediated MARCKS inhibition had no significant effect on inside-out β 2 -integrin activation. MANS treatment significantly attenuated ICAM-1/Mn 2+ -stimulated static adhesion, cell spreading and β 2 -integrin clustering, suggesting a role for MARCKS function in outside-in β 2 -integrin activation. Additional work is needed to better understand the molecular mechanisms of MARCKS role in outside-in β 2 -integrin activation and signaling.
ISSN:1933-6918
1933-6926
DOI:10.1080/19336918.2023.2233204