NDLI: Inhibition of MLC$_{20}$ Phosphorylation Downstream of Ca$^{2+}$ and RhoA: A Novel Mechanism Involving Phosphorylation of Myosin Phosphatase Interacting Protein (M-RIP) by PKG and Stimulation of MLC Phosphatase Activity

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Inhibition of MLC$_{20}$ Phosphorylation Downstream of Ca$^{2+}$ and RhoA: A Novel Mechanism Involving Phosphorylation of Myosin Phosphatase Interacting Protein (M-RIP) by PKG and Stimulation of MLC Phosphatase Activity

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Inhibition of MLC$_{20}$ Phosphorylation Downstream of Ca$^{2+}$ and RhoA: A Novel Mechanism Involving Phosphorylation of Myosin Phosphatase Interacting Protein (M-RIP) by PKG and Stimulation of MLC Phosphatase Activity

Content Provider	Springer Nature Link
Author	Mahavadi, Sunila Nalli, Ancydimpy Al Shboul, Othman Murthy, Karnam S.
Copyright Year	2013
Abstract	Previous studies have shown that cGMP-dependent protein kinase (PKG) act on several targets in the contractile pathway to reduce intracellular Ca$^{2+}$ and/or augment RhoA-regulated myosin light chain phosphatase (MLCP) activity and cause muscle relaxation. Recent studies have identified a novel protein M-RIP that associates with MYPT1, the regulatory subunit of MLCP. Herein, we examine whether PKG enhance MLCP activity downstream of Ca$^{2+}$ and RhoA via phosphorylation of M-RIP in gastric smooth muscle cells. Treatment of permeabilized muscle cells with 10 μM Ca$^{2+}$ caused an increase in MLC$_{20}$ phosphorylation and muscle contraction, but had no effect on Rho kinase activity. Activators of PKG (GSNO or cGMP) decreased MLC$_{20}$ phosphorylation and contraction in response to 10 μM Ca$^{2+}$, implying existence of inhibitory mechanism independent of Ca$^{2+}$ and RhoA. The effect of PKG on Ca$^{2+}$-induced MLC$_{20}$ phosphorylation was attenuated by M-RIP siRNA. Both GSNO and 8-pCPT-cGMP induced phosphorylation of M-RIP; phosphorylation was accompanied by an increase in the association of M-RIP with MYPT1 and MLCP activity. Taken together, these results provide evidence that PKG induces phosphorylation of M-RIP and enhances its association with MYPT1 to augment MLCP activity and MLC$_{20}$ dephosphorylation and inhibits muscle contraction, downstream of Ca$^{2+}$- or RhoA-dependent pathways.
Starting Page	1
Ending Page	8
Page Count	8
File Format	PDF
ISSN	10859195
Journal	Cell Biochemistry and Biophysics
Volume Number	68
Issue Number	1
e-ISSN	15590283
Language	English
Publisher	Springer US
Publisher Date	2013-05-31
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Smooth muscle Relaxation cGMP-dependent protein kinase cGMP Biochemistry Pharmacology/Toxicology Biotechnology Cell Biology Biophysics and Biological Physics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Biochemistry Biophysics

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