Physiological roles ofpost-translational modifications of water channel aquaporin-5 in the salivary glands.

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Two types of post-translational modifications, phosphorylation and short-chain ubiquitination, of water channel aquaporin-5 (AQP5) were investigated in the salivary gland cells. We reported that AQP5 is rapidly and transiently phosphorylated at the plasma membrane through the cAMP signaling pathway and this phosphorylation may not be involved in the intracellular AQP5 trafficking. A role of Ca2+-induced short-chain ubiquitination of AQP5 could not be cleared because of technical difficulties, small amount of its ubiquitination and the constitutive internalization of AQP5. However, we found that phosphorylation and ubiquitination of AQP5 affect each other’s modification.