NDLI: Agonist-induced $Ca^{2+}$ Sensitization in Smooth Muscle: REDUNDANCY OF RHO GUANINE NUCLEOTIDE EXCHANGE FACTORS (RhoGEFs) AND RESPONSE KINETICS, A CAGED COMPOUND STUDY

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Agonist-induced $Ca^{2+}$ Sensitization in Smooth Muscle: REDUNDANCY OF RHO GUANINE NUCLEOTIDE EXCHANGE FACTORS (RhoGEFs) AND RESPONSE KINETICS, A CAGED COMPOUND STUDY

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Agonist-induced $Ca^{2+}$ Sensitization in Smooth Muscle: REDUNDANCY OF RHO GUANINE NUCLEOTIDE EXCHANGE FACTORS (RhoGEFs) AND RESPONSE KINETICS, A CAGED COMPOUND STUDY

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Somlyo, Avril V. Gutkind, J. Silvio Artamonov, Mykhaylo V. Momotani, Ko Stevenson, Andra Derewenda, Zygmunt S. Read, Paul W. Derewenda, Urszula Trentham, David R.
Description	Author Affiliation: Artamonov MV ( From the Departments of Molecular Physiology and Biological Physics and.)
Abstract	Many agonists, acting through G-protein-coupled receptors and G subunits of the heterotrimeric G-proteins, induce contraction of smooth muscle through an increase of [Ca(2+)]i as well as activation of the RhoA/RhoA-activated kinase pathway that amplifies the contractile force, a phenomenon known as Ca(2+) sensitization. G 12/13 subunits are known to activate the regulator of G-protein signaling-like family of guanine nucleotide exchange factors (RhoGEFs), which includes PDZ-RhoGEF (PRG) and leukemia-associated RhoGEF (LARG). However, their contributions to Ca(2+)-sensitized force are not well understood. Using permeabilized blood vessels from PRG(-/-) mice and a new method to silence LARG in organ-cultured blood vessels, we show that both RhoGEFs are activated by the physiologically and pathophysiologically important thromboxane A2 and endothelin-1 receptors. The co-activation is the result of direct and independent activation of both RhoGEFs as well as their co-recruitment due to heterodimerization. The isolated recombinant C-terminal domain of PRG, which is responsible for heterodimerization with LARG, strongly inhibited Ca(2+)-sensitized force. We used photolysis of caged phenylephrine, caged guanosine 5'-O-(thiotriphosphate) (GTPÎ³S) in solution, and caged GTPÎ³S or caged GTP loaded on the RhoA·RhoGDI complex to show that the recruitment and activation of RhoGEFs is the cause of a significant time lag between the initial Ca(2+) transient and phasic force components and the onset of Ca(2+)-sensitized force.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	47
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-11-22
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Metabolism Guanine Nucleotide Exchange Factors Agonists Guanosine 5'-O-(3-Thiotriphosphate) Analogs & Derivatives Phenylephrine Rho Guanine Nucleotide Exchange Factors Animals Cell Line Gene Silencing Drug Effects Genetics Pharmacology Mice Mice, Knockout Organ Culture Techniques Protein Multimerization Protein Structure, Tertiary Rabbits Receptor, Endothelin A Receptors, Thromboxane A2, Prostaglandin H2 Recombinant Proteins Rho GTP-Binding Proteins Rho-Specific Guanine Nucleotide Dissociation Inhibitors RhoA GTP-Binding Protein Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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