[HTML][HTML] p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA
Y Koga, M Ikebe - Journal of Biological Chemistry, 2005 - ASBMB
p116 Rip was originally found to be a RhoA-binding protein, but its function has been
unknown. Here, we clarify the function of p116 Rip. Two critical findings were made. First, we
found that p116 Rip activated the GTPase activity of RhoA in vitro and that p116 Rip
overexpression in cells consistently diminished the epidermal growth factor-induced
increase in GTP-bound RhoA. Second, p116 Rip activated the myosin light chain
phosphatase (MLCP) activity of the holoenzyme. p116 Rip did not activate the catalytic …
unknown. Here, we clarify the function of p116 Rip. Two critical findings were made. First, we
found that p116 Rip activated the GTPase activity of RhoA in vitro and that p116 Rip
overexpression in cells consistently diminished the epidermal growth factor-induced
increase in GTP-bound RhoA. Second, p116 Rip activated the myosin light chain
phosphatase (MLCP) activity of the holoenzyme. p116 Rip did not activate the catalytic …