ADP-ribosylation of Rho enhances actin polymerization-coupled shape oscillations in human neutrophils.
Stimulated neutrophils exhibit coordinated sinusoidal oscillations in filamentous actin content and cellular shape. We investigated the effect of inhibition of the small G protein Rho on neutrophil actin polymerization, shape changes and oscillations using a genetically engineered toxin that enters cells and selectively ADP-ribosylates endogenous Rho. This treatment increased the amplitudes and frequencies of shape oscillations and duration of the oscillating transient. However, it had no effect on the initial actin polymerization and shape changes induced by N-formyl-Met-Leu-Phe. Regulation of these oscillations may be important for the control of neutrophil motility.
Ehrengruber
M U
MU
Theodor Kocher Institute, University of Bern, Switzerland.
Boquet
P
P
Coates
T D
TD
Deranleau
D A
DA
D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000209:Acute-Phase Proteins / Q000037:antagonists & inhibitors*; D000244:Adenosine Diphosphate; D000730:Androstadienes / Q000494:pharmacology; D048429:Cell Size / Q000187:drug effects; D003599:Cytoskeleton / Q000187:drug effects; D006801:Humans; D009504:Neutrophils / Q000378:metabolism*; D011994:Recombinant Proteins / Q000494:pharmacology; D014118:Toxins, Biological / Q000494:pharmacology*; D000077191:Wortmannin
D000199:Actins; D000209:Acute-Phase Proteins; D000730:Androstadienes; D011994:Recombinant Proteins; D014118:Toxins, Biological; C010781:acute-phase protein rho; D000244:Adenosine Diphosphate; D000077191:Wortmannin