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cotransporter is
mediated by regulation of cotransporter trafficking
1 Molecular Physiology Unit, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, and Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán Tlalpan 14000, Mexico City, Mexico; and 2 Department of Cellular and Molecular Physiology, Yale University Medical School, New Haven, Connecticut 06520
The murine
apical bumetanide-sensitive
Na+-K+-2Cl
cotransporter gene
(mBSC1) exhibits two spliced isoform products that differ at the
COOH-terminal domain. A long COOH-terminal isoform (L-mBSC1) encodes
the Na+-K+-2Cl cotransporter, and
a short isoform (S-mBSC1) exerts a dominant-negative effect on L-mBSC1
cotransporter activity that is abrogated by cAMP. However, the
mechanism of this dominant-negative effect was not clear. In this
study, we used confocal microscopic analysis of an enhanced green
fluorescent protein (EGFP) fusion construct (L-mBSC1-EGFP) expressed to
characterize the surface expression of the L-BSC1 isoform in
Xenopus laevis oocytes. Functional expression was also
assessed in L-mBSC1-injected oocytes by measuring the bumetanide-sensitive 86Rb+ uptake. Oocytes
injected with L-mBSC1-EGFP cRNA developed a distinct plasma
membrane-associated fluorescence that colocalized with the fluorescent
membrane dye FM 4-64. The fluorescence intensity in L-mBSC1-EGFP
oocytes did not change after cAMP was added to the extracellular
medium. In contrast, L-mBSC1-EGFP fluorescence intensity was reduced in
a dose-dependent manner, with coexpression of S-mBSC1. The inhibitory
effect of S-mBSC1 was abrogated by cAMP. Finally, the exocytosis
inhibitor colchicine blocked the effect of cAMP on the
L-mBSC1-EGFP/S-mBSC1-coinjected oocytes. All changes in L-mBSC1
surface expression correlated with modification of bumetanide-sensitive
86Rb+ uptake. Our data suggest that the
dominant-negative effect of S-mBSC1 on L-mBSC1 transport function is
due to the effects of the cotransporter on trafficking.
kidney; thick ascending limb; Xenopus laevis; oocytes; green fluorescent protein; NKCC2
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