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The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells.

Publication ,  Journal Article
Lopez, C; Métral, S; Eladari, D; Drevensek, S; Gane, P; Chambrey, R; Bennett, V; Cartron, J-P; Le Van Kim, C; Colin, Y
Published in: J Biol Chem
March 4, 2005

RhBG is a nonerythroid member of the Rhesus (Rh) protein family, mainly expressed in the kidney and belonging to the Amt/Mep/Rh superfamily of ammonium transporters. The epithelial expression of renal RhBG is restricted to the basolateral membrane of the connecting tubule and collecting duct cells. We report here that sorting and anchoring of RhBG to the basolateral plasma membrane require a cis-tyrosine-based signal and an association with ankyrin-G, respectively. First, we show by using a model of polarized epithelial Madin-Darby canine kidney cells that the targeting of transfected RhBG depends on a YED motif localized in the cytoplasmic C terminus of the protein. Second, we reveal by yeast two-hybrid analysis a direct interaction between an FLD determinant in the cytoplasmic C-terminal tail of RhBG and the third and fourth repeat domains of ankyrin-G. The biological relevance of this interaction is supported by two observations. (i) RhBG and ankyrin-G were colocalized in vivo in the basolateral domain of epithelial cells from the distal nephron by immunohistochemistry on kidney sections. (ii) The disruption of the FLD-binding motif impaired the membrane expression of RhBG leading to retention on cytoplasmic structures in transfected Madin-Darby canine kidney cells. Mutation of both targeting signal and ankyrin-G-binding site resulted in the same cell surface but nonpolarized expression pattern as observed for the protein mutated on the targeting signal alone, suggesting the existence of a close relationship between sorting and anchoring of RhBG to the basolateral domain of epithelial cells.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

March 4, 2005

Volume

280

Issue

9

Start / End Page

8221 / 8228

Location

United States

Related Subject Headings

  • Tyrosine
  • Two-Hybrid System Techniques
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Rats
  • Protein Structure, Tertiary
  • Mutation
  • Mutagenesis
  • Molecular Sequence Data
  • Microscopy, Fluorescence
 

Citation

APA
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Lopez, C., Métral, S., Eladari, D., Drevensek, S., Gane, P., Chambrey, R., … Colin, Y. (2005). The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells. J Biol Chem, 280(9), 8221–8228. https://doi.org/10.1074/jbc.M413351200
Lopez, Claude, Sylvain Métral, Dominique Eladari, Stéphanie Drevensek, Pierre Gane, Régine Chambrey, Vann Bennett, Jean-Pierre Cartron, Caroline Le Van Kim, and Yves Colin. “The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells.J Biol Chem 280, no. 9 (March 4, 2005): 8221–28. https://doi.org/10.1074/jbc.M413351200.
Lopez, Claude, et al. “The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells.J Biol Chem, vol. 280, no. 9, Mar. 2005, pp. 8221–28. Pubmed, doi:10.1074/jbc.M413351200.
Lopez C, Métral S, Eladari D, Drevensek S, Gane P, Chambrey R, Bennett V, Cartron J-P, Le Van Kim C, Colin Y. The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells. J Biol Chem. 2005 Mar 4;280(9):8221–8228.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

March 4, 2005

Volume

280

Issue

9

Start / End Page

8221 / 8228

Location

United States

Related Subject Headings

  • Tyrosine
  • Two-Hybrid System Techniques
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Rats
  • Protein Structure, Tertiary
  • Mutation
  • Mutagenesis
  • Molecular Sequence Data
  • Microscopy, Fluorescence