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J Biol Chem, Vol. 274, Issue 8, 4934-4938, February 19, 1999
From the The antidiuretic hormone arginine-vasopressin
(AVP) regulates water reabsorption in renal collecting duct principal
cells by inducing a cAMP-dependent translocation of water
channels (aquaporin-2, AQP-2) from intracellular vesicles into the
apical cell membranes. In subcellular fractions from primary cultured
rat inner medullary collecting duct (IMCD) cells, enriched for
intracellular AQP-2-bearing vesicles, catalytic protein kinase A (PKA)
subunits and several protein kinase A anchoring proteins (AKAPs) were
detected. In nonstimulated IMCD cells the majority of AQP-2 staining
was detected intracellularly but became mainly localized within the
cell membrane after stimulation with AVP or forskolin. Quantitative
analysis revealed that preincubation of the cells with the synthetic
peptide S-Ht31, which prevents the binding between AKAPs and regulatory subunits of PKA, strongly inhibited AQP-2 translocation in response to
forskolin. Preincubation of the cells with the PKA inhibitor H89 prior
to forskolin stimulation abolished AQP-2 translocation. In contrast to
H89, S-Ht31 did not affect the catalytic activity of PKA. These data
demonstrate that not only the activity of PKA, but also its tethering
to subcellular compartments, are prerequisites for
cAMP-dependent AQP-2 translocation.
Protein Kinase A Anchoring Proteins Are Required for
Vasopressin-mediated Translocation of Aquaporin-2 into Cell
Membranes of Renal Principal Cells
,,,, and¶
Forschungsinstitut für Molekulare
Pharmakologie, Alfred-Kowalke-Strasse 4, D-10315 Berlin,
Germany and the ¶ Freie Universität Berlin, Institut
für Pharmakologie, Thielallee 67-73, D-14195 Berlin,
Germany
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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