Impaired contractility and detrusor hypertrophy in cavin-1-deficient mice

Vasopressin-induced mouse urethral contraction is modulated by caveolin-1

“…6C). In keeping with prior reports in the bladder (Karbalaei et al, 2012), cavin-1 (Fig. 6D) and cavin-3 (Fig.…”

“…Given the apparently high cavin-3/cavin-2 expression ratio in smooth muscle tissues, it will be of interest to examine the impact of cavin-3 deletion on smooth muscle function in future work. It may however be difficult to dissect the role of Cav1 from that of cavin-1 and cavin-3 because these proteins affect each other's stability in smooth muscle (Karbalaei et al, 2012;Swärd et al, 2013).…”

The N-terminal leucine-zipper motif in PTRF/cavin-1 is essential and sufficient for its caveolae-association

“…Since the identification of PTRF and cavin-1 as the same protein [4,6], its function in plasma membrane caveolae has become the focal point for studying PTRF/ cavin-1. The recent works of cavin-1 raise substantial questions about its caveolae-independent functions in nuclei, especially no phenotypic defect related to ribosomal RNA synthesis has been identified in cavin-1 À/À mice [12][13][14]24,25]. Even in human clinical research, Cavin-1 deficient patients are only with muscle related diseases and metabolic diseases [26][27][28][29].…”

“…However, they breed very differently. Caveolin-1 À/À mice breed normally whereas cavin-1 À/À mice exhibit a high perinatal lethality [25]. Their phenotypic similarities can be attributed to the loss of caveolae or membrane functional disruption.…”

Cavin-3 (PRKCDBP) deficiency reduces the density of caveolae in smooth muscle

“…Whether cavin-3 is degraded by ablation of caveolae might be cell-type-dependent and the knockdown of cavin-1 has been found to destabilize cavin-3 in 3T3-L1 cells but hardly has any effect on heart and liver (Bastiani et al 2009). Our own work on cavin-1-deficient urinary bladders (Karbalaei et al 2012) and small mesenteric arteries (Sward et al 2014) has demonstrated the reduction of cavin-3, together with all caveolins. From these observations, we infer that cavin-3 contributes to higher-order protein assemblies in some cells but not in others and that this is dictated, at least in part, by its tissue concentration.…”