Study of F-actin interaction with planar and liposomal bilayer phospholipid membranes.
Interaction of the cytoskeletal protein F-actin with planar bilayer lipid membrane (BLM) induced formation of single ionic channels in both NaCl and KCl bathing solutions. We also recorded noiselike high-currentjumps with a mean conductivity of approximately 160 pS, which might represent the simultaneous opening and closing of several channels of lower conductivity. The ratio of cation to anion permeabilities (Pc/Pa) of the BLM with many channels in KCl was 26 +/- 2. Freeze-fracture electron microscopy revealed fibrillar-like structures on the hydrophobic surfaces of liposomal membranes. We also observed some structural features giving evidence for the penetration of F-actin fibers through an artificial phospholipid membrane. We suggest that the F-actin/lipids complexes can transmit electric signals in synaptic and other intercellular contacts.
Grigoriev
P A
PA
Institute of Cell Biophysics, Russian Academy of Science, Pushchino.
Tarahovsky
Y S
YS
Pavlik
L L
LL
Udaltsov
S N
SN
Moshkov
D A
DA
D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D005614:Freeze Fracturing; D066298:In Vitro Techniques; D007473:Ion Channels / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism*; D008081:Liposomes; D008564:Membrane Potentials; D008854:Microscopy, Electron; D010743:Phospholipids / Q000737:chemistry / Q000378:metabolism*; D011817:Rabbits
D000199:Actins; D007473:Ion Channels; D008051:Lipid Bilayers; D008081:Liposomes; D010743:Phospholipids