Rh. Sohn et Pj. Goldschmidtclermont, PROFILIN - AT THE CROSSROADS OF SIGNAL-TRANSDUCTION AND THE ACTIN CYTOSKELETON, BioEssays, 16(7), 1994, pp. 465-472
Despite its small size, profilin is an amazingly diverse and sophistic
ated protein whose precise role in cells continues to elude the unders
tanding of researchers 15 years after its discovery. Its ubiquity, abu
ndance and necessity for life in more evolved organisms certainly spea
ks for its extreme importance in cell function. So far, three ligands
for profilin have been well-characterized in vitro: actin monomers, me
mbrane polyphosphoinositides and poly-L-proline. In the years followin
g its discovery, profilin's role in vivo progressed from that of a sim
ple actin-binding protein which inhibits actin polymerization, to one
which, as an important regulator of the cytoskeleton, can even promote
actin polymerization under the appropriate circumstances. In addition
, interactions with components of the phosphatidylinositol cycle and t
he RAS pathway in yeast implicate profilin as an important link throug
h which the actin cytoskeleton is able to communicate with major signa
ling pathways.