1997
DOI: 10.1006/bbrc.1997.6537
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Molecular Cloning and Expression Analysis of RatRgs12andRgs14

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Cited by 110 publications
(111 citation statements)
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“…RGS can participate in many other protein-protein interactions via amino-and carboxylterminal extensions from the RGS domain (14). These likely serve to coordinate signaling between heterotrimeric G proteins and low molecular weight Ras superfamily G proteins (36,37) and between pairs of heterotrimeric G proteins (38,39). They can also cause signal-dependent translocation of other types of regulatory molecules to the site of active G␣ subunits (40) and may play a role in nuclear processes (33).…”
Section: S]gtp␥s Binding a And B Rgs-enhanced [mentioning
confidence: 99%
“…RGS can participate in many other protein-protein interactions via amino-and carboxylterminal extensions from the RGS domain (14). These likely serve to coordinate signaling between heterotrimeric G proteins and low molecular weight Ras superfamily G proteins (36,37) and between pairs of heterotrimeric G proteins (38,39). They can also cause signal-dependent translocation of other types of regulatory molecules to the site of active G␣ subunits (40) and may play a role in nuclear processes (33).…”
Section: S]gtp␥s Binding a And B Rgs-enhanced [mentioning
confidence: 99%
“…The R12 subfamily, composed of RGS12 and RGS14 (Snow et al, 1997), contain a second G␣-interacting region, the GoLoco motif, which has GDI activity toward G␣ i subunits (Kimple et al, 2001;Willard et al, 2004). R12 subfamily members also have a pair of Ras-binding domains (RBDs; Ponting, 1999), suggesting that these proteins may integrate signaling pathways involving both heterotrimeric and monomeric G-proteins.…”
Section: Introductionmentioning
confidence: 99%
“…Multiple splice variants for RGS12 and RGS14 have been reported (Snow et al, 1997;Chatterjee and Fisher, 2000b;Martin-McCaffrey et al, 2004). In addition to the RGS/RBD/GoLoco domain core, the long RGS12 splice variant has an N-terminal PDZ (PSD-95/Dlg/ZO-1) domain capable of binding the interleukin (IL) -8 receptor B (CXCR2) or its own C-terminus (Snow et al, 1998) and a phosphotyrosinebinding (PTB) domain that associates with tyrosine-phosphorylated N-type calcium channels (Schiff et al, 2000;Richman et al, 2005).…”
Section: Introductionmentioning
confidence: 99%
“…One particular family member, RGS14, is uniquely situated to regulate signaling pathways involved with synaptic plasticity. Originally identified as a binding partner for Rap GTPases (15,16), RGS14 has binding domains for multiple signaling proteins including active Gαi/o-GTP (RGS domain), Ras/Rap GTPases [tandem Ras Binding Domains (RBDs)] and for inactive Gαi1-GDP and Gαi3-GDP [a single G protein Regulatory (GPR) motif] (15)(16)(17)(18)(19)(20). Most recently, we have shown that RGS14 can act as a scaffold to assemble Gαi, H-Ras, and Raf kinases, in turn, to integrate G protein and ERK/MAPK signaling pathways and inhibit growth factor receptor signaling (21).…”
mentioning
confidence: 99%