GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:8662509
| Citation |
Kimura, K, Ito, M, Amano, M, Chihara, K, Fukata, Y, Nakafuku, M, Yamamori, B, Feng, J, Nakano, T, Okawa, K, Iwamatsu, A and Kaibuchi, K (1996) Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase) Science 273:245-8 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
3T3 Cells; Actins/metabolism; Amino Acid Sequence; Animals; Cattle; GTP Phosphohydrolases/metabolism; GTP-Binding Proteins/metabolism; Intracellular Signaling Peptides and Proteins; Isopropyl Thiogalactoside/pharmacology; Mice; Molecular Sequence Data; Muscle Contraction; Muscle, Smooth/physiology; Myosin Light Chains/metabolism; Myosin-Light-Chain Phosphatase; Oxazoles/pharmacology; Phosphoprotein Phosphatases/antagonists & inhibitors; Phosphoprotein Phosphatases/metabolism; Phosphorylation; Protein-Serine-Threonine Kinases/metabolism; rho-Associated Kinases; rhoA GTP-Binding Protein |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
See also
References
See Help:References for how to manage references in GONUTS.
