AFAP-1L1 activators include Phorbol 12-myristate 13-acetate (PMA), a known activator of protein kinase C (PKC), and a key player in signal transduction pathways that regulate numerous cellular functions, including gene expression, cell proliferation, and apoptosis. When PMA binds to PKC, it prompts the enzyme to phosphorylate various proteins, including AFAP-1L1. This phosphorylation enhances AFAP-1L1's ability to bind to actin filaments, thereby facilitating actin cytoskeleton reorganization which is critical for cell morphology, motility, and adhesion.
Calpeptin, a calpain inhibitor, works by preserving the integrity of proteins that calpain would otherwise cleave. By protecting AFAP-1L1 from calpain-mediated degradation, Calpeptin indirectly maintains the protein's functional state. This preservation is crucial for AFAP-1L1's role in actin filament organization and the linking of signaling pathways to cytoskeletal dynamics, impacting various cellular processes such as migration and structural maintenance.
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