Regulation of pollen tube growth is known to involve alterations in in
tracellular calcium levels and phosphoinositide signaling, although th
e mechanisms involved are unclear. However, it appears likely that pol
lination events involve a complex interplay between signaling pathways
and components of the actin cytoskeleton in pollen. In many eukaryoti
c cells, actin binding proteins function as stimulus-response modulato
rs, translating signals into alterations in the cytoplasmic architectu
re. In this study, we examined whether profilin, which is a member of
this class of signaling intermediate, might play a similar role in pol
len. We have analyzed the functional properties of native profilin fro
m pollen of Papaver rhoeas and have investigated the effects of profil
in on the phosphorylation of pollen proteins in vitro by adding a slig
ht excess of profilin to cytosolic pollen extracts. We present clear e
vidence that profilin interacts with soluble pollen components, result
ing in dramatic alterations in the phosphorylation of several proteins
. We also show, albeit in vitro, the involvement of profilin in modula
ting the activity of a signaling component(s) affecting protein phosph
orylation. Our data, which suggest that pollen profilin can regulate a
ctin-based cytoskeletal protein assembly and protein kinase or phospha
tase activity, indicate a possible role for the involvement of profili
n in signaling pathways that may regulate pollen tube growth.