The expression of a major cellular substrate for protein kinase C, the MARCKS protein, is regulated in a cell-, tissue-, and developmental stage-specific fashion; in addition, this expression can be stimulated acutely by various cytokines in certain cell types (1). As a filamentous (F) actin crosslinking protein, MARCKS binds to actin, calmodulin, and synapsin. In murine, MARCKS binding activity is regulated by PKC phosphorylation at Ser152, 156, and 163 of MARCKS during macrophage and neutrophil activation, growth factor-dependent mitogenesis and neurosecretion. After phospholyation, MARCKS is redistributed from plasma membrane to cytoplasm and is involved in leukocyte motility. MARCKS may be a regulated crossbridge between actin and the plasma membrane, and modulation of the actin crosslinking activity of the MARCKS protein by calmodulin and phosphorylation represents a potential convergence of the calcium-calmodulin and PKC signal transduction pathways in the regulation of the actin cytoskeleton (2).
Suitable for use in Western Blot and Immunoprecipitation. Other applications not tested.
Western Blot: 1:1000