Truncated form of VACM-1/cul-5 with an extended 3′ untranslated region stimulates cell growth via a MAPK-dependent pathway

Sartor, Ashleigh; Kossoris, J.; Wilcox, R. A.; Shearer, R. L.; Zeneberg, A.E.; Zhao, Ping; Lazdins, Inara B.; Burnatowska-Hledin, Maria

doi:10.1016/j.bbrc.2006.02.197

Cited by 5 publications

(2 citation statements)

References 25 publications

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“…This vasopressin-activated Ca 2+ mobilizing (VACM-1) receptor has no amino acid sequence homology with the traditional vasopressin receptors and is expressed in numerous endothelial cells (BurnatowskaHledin et al, 1999), as well as in the renal medullary collected tubules. It is homologous with a newly discovered cullin family of proteins which are involved in the regulation of cellular signalling by calcium, cyclic AMP (Burnatowska-Hledin et al, 2000) and the MAPK-dependant pathway (Sartor et al, 2006). On the basis of molecular recognition theory, this predicts that binding domains of peptides and their corresponding receptor binding domains evolved from complementary strands of genes.…”

Section: Are There Other Vasopressin Receptors?mentioning

confidence: 99%

Vasopressin Receptors, the Signalling Cascade and Mechanisms of Action

Hanoune

2009

Perspectives on Vasopressin

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Section: Are There Other Vasopressin Receptors?mentioning

confidence: 99%

Vasopressin Receptors, the Signalling Cascade and Mechanisms of Action

Hanoune

2009

Perspectives on Vasopressin

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“…The cRNA probe used in our study is directed against the N-terminus of VACM-1 cDNA sequence. We have observed that a truncated form of VACM-1 protein lacking the N-terminus sequence of VACM-1 protein may be expressed in the kidney [38]. Whether the levels of the truncated form of VACM-1 are increased in specific regions of the kidney and are controlled by the hydration status remain to be determined.…”

Section: Discusionmentioning

confidence: 99%

Aquaporin-2 Levelsin vitroandin vivoare Regulated by VACM-1, a Cul 5 Gene

Schultz

Andresen

et al. 2012

Cell Physiol Biochem

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Background: In the renal collecting duct, vasopressin regulates water permeability by a process that involves stimulation of adenylyl cyclase activity, cAMP production and subsequent translocation of water channel aquaporin-2 (AQP2) into the apical plasma membrane. We have previously shown that in cos 1 cells in vitro, both adenylyl cyclase activity and cAMP production can be regulated by VACM-1, a cul 5 gene that forms complexes involved in protein ubiquitination and subsequent degradation. Methods: To extend these observations further, the effects of changes in hydration state on the expression of VACM-1 at the mRNA and the protein level were examined in rats deprived of water (WD) for 24 hrs. Results: In the kidney of WD rats Western blot analyses of kidney tissue showed that the decrease in VACM-1 protein concentration was correlated with the increase in the AQP2 protein level. The immunostaining data suggested that VACM-1/cul5 may be decreased in renal collecting duct but increases in the vasculature of the inner medullary region in response to WD. To determine the possible consequences of the WD dependent decrease in VACM-1/cul5, we next examined the effects of VACM-1 expression on AQP2 protein in vitro. Immunocytochemistry and Western blot analyses data indicate that VACM-1/cul5 expression in MDCK line stably expressing AQP2 gene and in cos 1 cells co-transfected with the AQP2 and VACM-1/cul5 cDNAs decreased AQP2 protein concentration when compared to the vector transfected control groups. Conclusion: In summary, our data demonstrate that VACM-1 is involved in the regulation of AQP2 protein concentration and may play a role in regulating water balance.

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VACM-1/cul5 expression in vascular tissue in vivo is induced by water deprivation and its expression in vitro regulates aquaporin-1 concentrations

Johnson

Andresen

et al. 2012

Cell Tissue Res

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VACM-1, a cul5 gene product, when overexpressed in vitro, has an antiproliferative effect. In vivo, VACM-1/cul5 is present in tissues involved in the regulation of water balance. Neither proteins targeted for VACM-1/cul5-specific degradation nor factors that may regulate its expression in those tissues have been studied. To identify genes that may be misregulated by VACM-1 cDNA, we performed microarray analysis. Our results indicate that in cos-1 cells transfected with VACM-1 cDNA, mRNA levels for several genes, including AQP1, were decreased when compared to the control group. Our results also indicate that in cos-1 cells transfected with VACM-1 cDNA, endogenous AQP1 protein was decreased about 6-fold when compared to the controls. To test the hypothesis that VACM-1/cul5 may be regulated by conditions that compromise water homeostasis in vivo, we determined if 24 h of water deprivation affects VACM-1/cul5 levels or the effect of VACM-1/cul5 on AQP1. VACM-1 mRNA and protein levels were significantly higher in rat mesenteric arteries, skeletal muscle and the heart ventricle but not in the heart atrium from 24-h water-deprived rats when compared to the controls. Interestingly, 24 h of water deprivation increased modification of VACM-1 by an ubiquitin-like protein, Nedd8, essential for cullin-dependent E3 ligase activity. Although water deprivation did not significantly change AQP1 levels in the mesenteric arteries, AQP1 protein concentrations were inversely correlated with the ratio of the VACM-1 to Nedd8-modified VACM-1. These results suggest that VACM-1/cul5 may regulate endothelial AQP1 concentration both in vivo and in vitro.

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Truncated form of VACM-1/cul-5 with an extended 3′ untranslated region stimulates cell growth via a MAPK-dependent pathway

Cited by 5 publications

References 25 publications

Vasopressin Receptors, the Signalling Cascade and Mechanisms of Action

Vasopressin Receptors, the Signalling Cascade and Mechanisms of Action

Aquaporin-2 Levelsin vitroandin vivoare Regulated by VACM-1, a Cul 5 Gene

VACM-1/cul5 expression in vascular tissue in vivo is induced by water deprivation and its expression in vitro regulates aquaporin-1 concentrations

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