Cellular morphology, adhesion, and motility occur through dynamic reorganization of actin-based superstructures. Actin-binding proteins are critical for regulating actin polymerization and superstructure formation. The Arp2/3 complex is an actin polymerization-inducing complex that includes Arp2, Arp3, p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. Several nucleation promoting factors, such as WASP and coronin, regulate the activity of the Arp2/3 complex. In addition, the Arp2/3 complex may be regulated by phosphorylation of specific subunits in the complex. Arp2 has two phosphosites, Thr-237 and Thr-238, that are evolutionarily conserved, and are phosphorylated along with Tyr-202 in response to growth factor stimulation. These phosphorylation events may regulate binding to the pointed end of actin filaments, and alanine substitutions of these Arp2 phosphosites inhibit membrane protrusions. Thus, phosphorylation may be another mode of Arp2/3 complex regulation in addition to the activity of nucleation-promoting factors.
References
Soderling, S.H. (2009). Sci Signal. 2(55):pe5 (Review). LeClaire, L.L. et al (2008). J Cell Biol. 182(4):647.Kelleher, J.F. et al. (1995). J Cell Biol. 131(2):385.
Immunocytochemical labeling of Arp3 in aldehyde-fixed and NP-40-permeabilized rat PC12 cells differentiated with NGF. The cells were labeled with rabbit polyclonal anti-Arp3 (C-terminal region) (AP4581) in the absence (left) or presence (right) of blocking peptide (AX4585). The antibody was detected using appropriate secondary antibody conjugated to DyLight® 594.
*For more information, see UniProt Accession P61158
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.
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