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transfected, unstimulated MDCK cells, wild-type AQP2 (stained green) appeared in a punctate pattern distributed throughout the subapical region (Figure 4B, left column photomicrographs), consistent with vesicular compartmentalization. AQP2-F204V, on the other hand, appeared in a punctate but perinuclear pattern (Figure 4B, third column). Upon stimulation with forskolin, a cAMP-dependent protein kinase activator, wild-type AQP2 translocated to the apical surface of polarized MDCK cells (Figure 4B, second column). Along the z-axis, the perinuclear distribution of AQP2-F204V was clearly seen, and this distribution is not altered by forskolin (Figure 4B, bottom row, two right columns). The perinuclear distribution of AQP2-F204V is consistent with an ER compartmentalization. To test the idea that AQP2-F204V localizes to the ER, we co-stained cells transfected with Aqp2F204V (cDNA) for AQP2 and an ER marker, calnexin (Figure 4C). Colocalization of calnexin with AQP2 was investigated directly, and it was found that 80% of all AQP2-F204V protein colocalized with calnexin. The remaining 20% appeared at the periphery of the ER, representing AQP2-F204V that had potentially progressed beyond the ER. This “ER escape” was consistent with the small proportion of mature, complex glycosylated, AQP2-F204V in mutant kidneys (see Figure 3A)."}