Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells

Gouraud, Sabine S.; Laera, A.F.; Calamita, Giuseppe; Carmosino, Monica; Procino, Giuseppe; Rossetto, Ornella; Mannucci, Roberta; Rosenthal, Walter; Svelto, María; Valenti, Giovanna

doi:10.1242/jcs.00053

Cited by 69 publications

(39 citation statements)

References 37 publications

(41 reference statements)

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“…In basal conditions, AQP2 was localized mainly intracellularly, whereas incubation with forskolin caused translocation of AQP2 to the apical plasma membrane, as described previously and confirmed using an antibody that recognizes the extracellular C-loop of the AQP2 protein (23,32,33) ( reconstruction in the inset). For clarifying whether inhibition of AQP2 translocation by BK requires PLC activation, CD8 cells were pretreated with U73122.…”

Section: Bk Antagonizes Forskolin-induced Aqp2 Translocationsupporting

confidence: 79%

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

Tamma¹,

Carmosino²,

Svelto³

et al. 2005

Journal of the American Society of Nephrology

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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.

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Section: Bk Antagonizes Forskolin-induced Aqp2 Translocationsupporting

confidence: 79%

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

Tamma¹,

Carmosino²,

Svelto³

et al. 2005

Journal of the American Society of Nephrology

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“…Cyclic AMP Decreases the Interaction of AKAP18␦ with Regulatory PKA Subunits-To obtain further evidence for the involvement of AKAP18␦ in the AQP2 shuttle, FRET experiments were carried out with a rabbit cortical collecting duct cell line stably expressing AQP2 (CD8 cells). After stimulation of CD8 cells with forskolin, a direct activator of adenylyl cyclase, AQP2 translocates to the apical plasma membrane (29,33,34,56). To monitor the interaction of AKAP18␦ with PKA, CD8 cells were transiently co-transfected with plasmids encoding AKAP18␦-CFP and RII␣-YFP.…”

Section: Fig 3 Akap18␦ Functions As An Akap In Vivomentioning

confidence: 99%

“…Whereas VAMP2 and dynein appear to be exclusively located on the vesicles, Hrs-2 appears to be present on both the vesicles and at the plasma membrane. VAMP2 is required for fusion of AQP2-bearing vesicles with the plasma membrane (56), and Hrs-2 may play a modulatory role in the fusion process (57). Dynein may be involved in the vesicular transport of AQP2-bearing vesicles to the plasma membrane along microtubules (58).…”

Section: Fig 3 Akap18␦ Functions As An Akap In Vivomentioning

confidence: 99%

Identification of a Novel A-kinase Anchoring Protein 18 Isoform and Evidence for Its Role in the Vasopressin-induced Aquaporin-2 Shuttle in Renal Principal Cells

Henn

Edemir

Stefan

et al. 2004

Journal of Biological Chemistry

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130

166

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“…8). GLUT4 and AQP2 translocation share some similarities such as the requirement for the v-SNARE synaptobrevin-2 in fusion with the plasma membrane (8,9). Nevertheless, there are important differences.…”

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confidence: 99%

Glycosylation Is Important for Cell Surface Expression of the Water Channel Aquaporin-2 but Is Not Essential for Tetramerization in the Endoplasmic Reticulum

Hendriks¹,

Koudijs²,

Balkom³

et al. 2004

Journal of Biological Chemistry

137

115

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Aquaporin-2 (AQP2) is a pore-forming protein that is required for regulated reabsorption of water from urine. Mutations in AQP2 lead to nephrogenic diabetes insipidus, a disorder in which functional AQP2 is not expressed on the apical cell surface of kidney collecting duct principal cells. The mechanisms and pathways directing AQP2 from the endoplasmic reticulum to the Golgi complex and beyond have not been defined. We found that ϳ25% of newly synthesized AQP2 is glycosylated. Nonglycosylated and complex-glycosylated wildtype AQP2 are stable proteins with a half-life of 6 -12 h and are both detectable on the cell surface. We show that AQP2 forms tetramers in the endoplasmic reticulum during or very early after synthesis and reaches the Golgi complex in 1-1.5 h. We also report that glycosylation is neither essential for tetramerization nor for transport from the endoplasmic reticulum to the Golgi complex. Instead, the N-linked glycan is important for exit from the Golgi complex and sorting of AQP2 to the plasma membrane. These results are important for understanding the molecular mechanisms responsible for the intracellular retention of AQP2 in nephrogenic diabetes insipidus.

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Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells

Cited by 69 publications

References 37 publications

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

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

Identification of a Novel A-kinase Anchoring Protein 18 Isoform and Evidence for Its Role in the Vasopressin-induced Aquaporin-2 Shuttle in Renal Principal Cells

Glycosylation Is Important for Cell Surface Expression of the Water Channel Aquaporin-2 but Is Not Essential for Tetramerization in the Endoplasmic Reticulum

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