Regular ArticleInhibition of Retinal Guanylyl Cyclase by the RGS9-1 N-Terminus☆
References (30)
- et al.
J. Biol. Chem.
(1994) - et al.
Trends Neurosci.
(1996) - et al.
J. Biol. Chem.
(1994) - et al.
J. Biol. Chem.
(1994) - et al.
J. Biol. Chem.
(2000) - et al.
J. Biol. Chem.
(2000) - et al.
J. Biol. Chem.
(1990) - et al.
Neuron
(1998) - et al.
Trends Cell Biol.
(1999) - et al.
Gene
(1999)
J. Biol. Chem.
J. Biol. Chem.
Neuron
Neuron
Cited by (10)
Regulators of G-Protein-Signaling Proteins: Negative Modulators of G-Protein-Coupled Receptor Signaling
2015, International Review of Cell and Molecular BiologyCitation Excerpt :It has also been suggested that the Gβ5•RGS complex might bind to inactive Gα-subunits and then joining them to a larger GPCR complex that positions the RGS protein in the area where its GAP activity is required (Siderovski and Willard, 2005; Sondek and Siderovski, 2001). The GGL domain has been also associated with other functions namely: RGS6 GGL domain interaction with SCG10 neuronal protein to enhance differentiation (Liu et al., 2002), and to inhibit a transcriptional repressor named DMAP1 (Liu and Fisher, 2004), to suppress the RGS9-1 inhibitory ability of guanylyl cyclase activity (Yu et al., 2001). The R7 family members of RGS proteins also interact with the membrane anchoring proteins R7BP and R9AP.
How Regulators of G Protein Signaling Achieve Selective Regulation
2007, Journal of Molecular BiologyMammalian RGS proteins: Multifunctional regulators of cellular signalling
2006, Seminars in Cell and Developmental BiologyRegulators of G-protein signalling: Multifunctional proteins with impact on signalling in the cardiovascular system
2003, Pharmacology and TherapeuticsSignal-dependent translocation of transducin, RGS9-1-Gβ5L complex, and arrestin to detergent-resistant membrane rafts in photoreceptors
2002, Current BiologyCitation Excerpt :Since PDEγ has affinity for the transition state of transducin, and a portion of PDE is associated with raft, it could potentially act as an anchor to recruit the RGS9-1 complex [8, 10]. We can also speculate that RGS9-1 is anchored to the raft via another molecule, for example, guanylate cyclase, which is permanently raft associated (Figure 1B) and is reported to bind RGS9-1 [11, 12]. Another possibility is that RGS9-1 phosphorylation [13, 14] plays a role in its association with rafts.
- ☆
This work was supported by a National Institutes of Health Grant EY09631 and an unrestricted grant from Research to Prevent Blindness.
- 1
To whom correspondence should be addressed at Kresge Eye Institute, Wayne State University, School of Medicine, 4717 St. Antoine Street, Detroit, MI 48201. Fax: 313-577-0238. E-mail: [email protected].