Potential roles of heterotrimeric G proteins of the endomembrane system

Nürnberg, Bernd; Ahnert‐Hilger, Gudrun

doi:10.1016/0014-5793(96)00584-4

Cited by 56 publications

(41 citation statements)

References 73 publications

(62 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is interesting that plasma membrane localization of G␣13 required palmitoylation, a posttranslational dynamic and reversible modification (35). Moreover, G proteins, traditionally thought to be transducer molecules confined to the plasma membrane, are also present on intracellular vesicles as ␣␤␥ heterotrimers, and we and others have suggested that they participate in various intracellular transport pathways (32,36). In NIH3T3 cells, transfection with the constitutively active G␣13 greatly increased the affinity between G␣13 and F-actin, indicating that affinity between F-actin and G␣13 might be considered an important indicator of G␣13 activity (25).…”

Section: Bk Modulates G␣13 Cellular Distributionmentioning

confidence: 99%

Bradykinin Signaling Counteracts cAMP-Elicited Aquaporin 2 Translocation in Renal Cells

Tamma¹,

Carmosino²,

Svelto³

et al. 2005

Journal of the American Society of Nephrology

View full text Add to dashboard Cite

Bradykinin (BK) is one of the most important peptides regulating vascular tone, water, and ionic balance in the body, playing a key role in controlling BP. It is interesting that patients with essential hypertension excrete less BK than normotensive individuals. For elucidating the mechanism by which BK regulates renal water transport that contributes to its antihypertensive effect, aquaporin 2 (AQP2)-transfected collecting duct CD8 cells, expressing the BK type II receptor (BK2R), were used as an experimental model. In CD8 cells, BK pretreatment impaired forskolin-induced AQP2 translocation to the apical plasma membrane. For clarifying the signal transduction cascade associated with this effect, whether BK induced an increase in cytosolic calcium, via the G protein Gq, known to be coupled to BK2R, first was investigated. Spectrofluorometry using fura-2-AM revealed that 100 nM BK elicited a significant increase in Ca i , which was abolished by the receptor antagonist HOE-140. BK acts through BK2R coupled to both Gq and G␣13, a known upstream effector of Rho protein. In CD8 cells, BK causes an increase in Rho activity, likely as a result of G␣13 activation. This results in stabilization of the cortical F-actin network, thus impairing AQP2 trafficking. These effects counteract physiologic vasopressin stimulation, which instead has an opposite effect on actin network organization through Rho inactivation.

show abstract

Section: Bk Modulates G␣13 Cellular Distributionmentioning

confidence: 99%

Bradykinin Signaling Counteracts cAMP-Elicited Aquaporin 2 Translocation in Renal Cells

Tamma¹,

Carmosino²,

Svelto³

et al. 2005

Journal of the American Society of Nephrology

View full text Add to dashboard Cite

show abstract

“…33). We examined whether or not heterotrimeric G proteins are involved in the disassembly of the Golgi apparatus.…”

Section: Ndga Causes Disassembly Of the Golgi Apparatus In A Microtubmentioning

confidence: 99%

Possible Involvement of Heterotrimeric G Proteins in the Organization of the Golgi Apparatus

Yamaguchi¹,

Yamamoto²,

Furuno³

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…Besides their plasma membrane location, heterotrimeric G proteins also are found on membranes of intracellular compartments along both the endocytic and secretory pathways where indirect evidence suggests they play several roles in membrane trafficking (Bomsel and Mostov, 1992;Helms, 1995;Nurnberg and Ahnert-Hilger, 1996;Stow and Heimann, 1998). One of the prototypical heterotrimeric G proteins, G␣s, the stimulatory subunit of heterotrimeric G proteins, has been suggested to regulate endocytic trafficking.…”

Section: Introductionmentioning

confidence: 99%

Regulation of Epidermal Growth Factor Receptor Degradation by Heterotrimeric Gαs Protein

Zheng

Lavoie

Tang

et al. 2004

MBoC

View full text Add to dashboard Cite

Heterotrimeric G proteins have been implicated in the regulation of membrane trafficking, but the mechanisms involved are not well understood. Here, we report that overexpression of the stimulatory G protein subunit (Gαs) promotes ligand-dependent degradation of epidermal growth factor (EGF) receptors and Texas Red EGF, and knock-down of Gαs expression by RNA interference (RNAi) delays receptor degradation. We also show that Gαs and its GTPase activating protein (GAP), RGS-PX1, interact with hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs), a critical component of the endosomal sorting machinery. Gαs coimmunoprecipitates with Hrs and binds Hrs in pull-down assays. By immunofluorescence, exogenously expressed Gαs colocalizes with myc-Hrs and GFP-RGS-PX1 on early endosomes, and expression of either Hrs or RGS-PX1 increases the localization of Gαs on endosomes. Furthermore, knock-down of both Hrs and Gαs by double RNAi causes greater inhibition of EGF receptor degradation than knock-down of either protein alone, suggesting that Gαs and Hrs have cooperative effects on regulating EGF receptor degradation. These observations define a novel regulatory role for Gαs in EGF receptor degradation and provide mechanistic insights into the function of Gαs in endocytic sorting

show abstract

Potential roles of heterotrimeric G proteins of the endomembrane system

Cited by 56 publications

References 73 publications

Bradykinin Signaling Counteracts cAMP-Elicited Aquaporin 2 Translocation in Renal Cells

Bradykinin Signaling Counteracts cAMP-Elicited Aquaporin 2 Translocation in Renal Cells

Possible Involvement of Heterotrimeric G Proteins in the Organization of the Golgi Apparatus

Regulation of Epidermal Growth Factor Receptor Degradation by Heterotrimeric Gαs Protein

Contact Info

Product

Resources

About