[Interaction of the beta1-subunit of G-proteins with the actin cytoskeleton].
Using immunoblotting with specific antibodies, we have identified beta 1- and beta 2-subunits of Gi-proteins in membrane and cytosolic fractions of pig lung. It has been shown that beta 1-subunit is present both in membrane and cytosolic fractions, whereas beta 2-subunit is associated only with membranes. Activation of membrane-bound G proteins with non-hydrolysable GTP analogues have led to partial release from membrane of beta 1-, but not beta 2-subunits. When depolymerisation of F-actin during fractionation was prevented, both beta 1- and beta 2-subunits were found in fraction containing total membranes and F-actin. Dialysis of this fraction into low ionic strength buffer caused depolymerization of the bulk of actin and release of about 1/4 of beta 1-subunits into solution. The data presented here suggest that distribution of beta 1-subunits between membrane and cytosol could depend on the state of actin cytoskeleton.
Grishin
A V
AV
Russian Cardiology Research Centre, Moscow, Russia.
Gerasimovskaia
E V
EV
Starikova
M G
MG
Panchenko
M P
MP
Nikashin
A V
AV
Tkachuk
V A
VA
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism*; D008168:Lung / Q000378:metabolism; D009994:Osmolar Concentration; D011485:Protein Binding; D013552:Swine
D000199:Actins; D019204:GTP-Binding Proteins
Vzaimodeĭstvie beta1-sub''edinits G-belkov s aktinovym tsitoskeletom.