Kimura K, Ito M, Amano M, Chihara K, Fukata Y, Nakafuku M, Yamamori B, Feng J, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K
Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-01, Japan.
Science. 1996 Jul 12;273(5272):245-8. doi: 10.1126/science.273.5272.245.
The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP.RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.
小GTP酶Rho与肌球蛋白轻链(MLC)磷酸化有关,MLC磷酸化会导致平滑肌收缩以及非肌肉细胞中肌动蛋白和肌球蛋白相互作用。鸟苷三磷酸(GTP)结合的活性形式RhoA(GTP.RhoA)特异性地与肌球蛋白磷酸酶的肌球蛋白结合亚基(MBS)相互作用,MBS可调节MLC的磷酸化程度。由GTP.RhoA激活的Rho相关激酶(Rho激酶)使MBS磷酸化,从而使肌球蛋白磷酸酶失活。在NIH 3T3细胞中过表达RhoA或激活RhoA会增加MBS和MLC的磷酸化。因此,Rho似乎通过Rho激酶的作用抑制肌球蛋白磷酸酶。