Phospho-proteomics:Article Title: Takis Anagnostopoulos Symposium: Renal and Epithelial Physiology and Pathophysiology
Article Snippet: 47 Phosphorylation and Ankyrine-G Binding of the C-Terminal Domain Regulate Targeting and Function of the Ammonium Transporter RhBG Fabien Sohet, Yves Colin, Sandrine Genetet, Pierre Ripoche, Sylvain Metral, Caroline Le van Kim, Claude Lopez INSERM, U665, Institut National de la Transfusion Sanguine, 6 Rue Alexandre Cabanel, Paris, F-75015, France; Université Paris7-Denis Diderot, Paris, F-75013, France RhBG, a human member of the Amt/Mep/Rh/superfamily of ammonium transporters, has been shown to facilitate NH3 transport and to be anchored to the basolateral plasma membrane of kidney epithelial cells, via ankyrin-G. We showed here that triple alanine substitution of the 419-FLD-421 sequence, which links the cytoplasmic C-terminal domain of RhBG to ankyrin-G, not only disrupted the interaction of RhBG with the spectrin-based skeleton but also delayed its cell surface expression and abolished its NH3 transport function in epithelial cell lines.
Binding Assay:Article Title: Takis Anagnostopoulos Symposium: Renal and Epithelial Physiology and Pathophysiology
Article Snippet: 47 Phosphorylation and Ankyrine-G Binding of the C-Terminal Domain Regulate Targeting and Function of the Ammonium Transporter RhBG Fabien Sohet, Yves Colin, Sandrine Genetet, Pierre Ripoche, Sylvain Metral, Caroline Le van Kim, Claude Lopez INSERM, U665, Institut National de la Transfusion Sanguine, 6 Rue Alexandre Cabanel, Paris, F-75015, France; Université Paris7-Denis Diderot, Paris, F-75013, France RhBG, a human member of the Amt/Mep/Rh/superfamily of ammonium transporters, has been shown to facilitate NH3 transport and to be anchored to the basolateral plasma membrane of kidney epithelial cells, via ankyrin-G. We showed here that triple alanine substitution of the 419-FLD-421 sequence, which links the cytoplasmic C-terminal domain of RhBG to ankyrin-G, not only disrupted the interaction of RhBG with the spectrin-based skeleton but also delayed its cell surface expression and abolished its NH3 transport function in epithelial cell lines.
Clinical Proteomics:Article Title: Takis Anagnostopoulos Symposium: Renal and Epithelial Physiology and Pathophysiology
Article Snippet: 47 Phosphorylation and Ankyrine-G Binding of the C-Terminal Domain Regulate Targeting and Function of the Ammonium Transporter RhBG Fabien Sohet, Yves Colin, Sandrine Genetet, Pierre Ripoche, Sylvain Metral, Caroline Le van Kim, Claude Lopez INSERM, U665, Institut National de la Transfusion Sanguine, 6 Rue Alexandre Cabanel, Paris, F-75015, France; Université Paris7-Denis Diderot, Paris, F-75013, France RhBG, a human member of the Amt/Mep/Rh/superfamily of ammonium transporters, has been shown to facilitate NH3 transport and to be anchored to the basolateral plasma membrane of kidney epithelial cells, via ankyrin-G. We showed here that triple alanine substitution of the 419-FLD-421 sequence, which links the cytoplasmic C-terminal domain of RhBG to ankyrin-G, not only disrupted the interaction of RhBG with the spectrin-based skeleton but also delayed its cell surface expression and abolished its NH3 transport function in epithelial cell lines.
Membrane:Article Title: Takis Anagnostopoulos Symposium: Renal and Epithelial Physiology and Pathophysiology
Article Snippet: 47 Phosphorylation and Ankyrine-G Binding of the C-Terminal Domain Regulate Targeting and Function of the Ammonium Transporter RhBG Fabien Sohet, Yves Colin, Sandrine Genetet, Pierre Ripoche, Sylvain Metral, Caroline Le van Kim, Claude Lopez INSERM, U665, Institut National de la Transfusion Sanguine, 6 Rue Alexandre Cabanel, Paris, F-75015, France; Université Paris7-Denis Diderot, Paris, F-75013, France RhBG, a human member of the Amt/Mep/Rh/superfamily of ammonium transporters, has been shown to facilitate NH3 transport and to be anchored to the basolateral plasma membrane of kidney epithelial cells, via ankyrin-G. We showed here that triple alanine substitution of the 419-FLD-421 sequence, which links the cytoplasmic C-terminal domain of RhBG to ankyrin-G, not only disrupted the interaction of RhBG with the spectrin-based skeleton but also delayed its cell surface expression and abolished its NH3 transport function in epithelial cell lines.
Sequencing:Article Title: Takis Anagnostopoulos Symposium: Renal and Epithelial Physiology and Pathophysiology
Article Snippet: 47 Phosphorylation and Ankyrine-G Binding of the C-Terminal Domain Regulate Targeting and Function of the Ammonium Transporter RhBG Fabien Sohet, Yves Colin, Sandrine Genetet, Pierre Ripoche, Sylvain Metral, Caroline Le van Kim, Claude Lopez INSERM, U665, Institut National de la Transfusion Sanguine, 6 Rue Alexandre Cabanel, Paris, F-75015, France; Université Paris7-Denis Diderot, Paris, F-75013, France RhBG, a human member of the Amt/Mep/Rh/superfamily of ammonium transporters, has been shown to facilitate NH3 transport and to be anchored to the basolateral plasma membrane of kidney epithelial cells, via ankyrin-G. We showed here that triple alanine substitution of the 419-FLD-421 sequence, which links the cytoplasmic C-terminal domain of RhBG to ankyrin-G, not only disrupted the interaction of RhBG with the spectrin-based skeleton but also delayed its cell surface expression and abolished its NH3 transport function in epithelial cell lines.
Expressing:Article Title: Takis Anagnostopoulos Symposium: Renal and Epithelial Physiology and Pathophysiology
Article Snippet: 47 Phosphorylation and Ankyrine-G Binding of the C-Terminal Domain Regulate Targeting and Function of the Ammonium Transporter RhBG Fabien Sohet, Yves Colin, Sandrine Genetet, Pierre Ripoche, Sylvain Metral, Caroline Le van Kim, Claude Lopez INSERM, U665, Institut National de la Transfusion Sanguine, 6 Rue Alexandre Cabanel, Paris, F-75015, France; Université Paris7-Denis Diderot, Paris, F-75013, France RhBG, a human member of the Amt/Mep/Rh/superfamily of ammonium transporters, has been shown to facilitate NH3 transport and to be anchored to the basolateral plasma membrane of kidney epithelial cells, via ankyrin-G. We showed here that triple alanine substitution of the 419-FLD-421 sequence, which links the cytoplasmic C-terminal domain of RhBG to ankyrin-G, not only disrupted the interaction of RhBG with the spectrin-based skeleton but also delayed its cell surface expression and abolished its NH3 transport function in epithelial cell lines.
|
