Involvement of Golgin-160 in cell surface transport of renal ROMK channel: co-expression of Golgin-160 increases ROMK currents
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Involvement of Golgin-160 in cell surface transport of renal ROMK channel: co-expression of Golgin-160 increases ROMK currents. / Bundis, Florian; Neagoe, Ioana; Schwappach, Blanche; Steinmeyer, Klaus.
in: CELL PHYSIOL BIOCHEM, Jahrgang 17, Nr. 1-2, 2006, S. 1-12.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Involvement of Golgin-160 in cell surface transport of renal ROMK channel: co-expression of Golgin-160 increases ROMK currents
AU - Bundis, Florian
AU - Neagoe, Ioana
AU - Schwappach, Blanche
AU - Steinmeyer, Klaus
PY - 2006
Y1 - 2006
N2 - The weak inward rectifier potassium channel ROMK is important for water and salt reabsorption in the kidney. Here we identified Golgin-160 as a novel interacting partner of the ROMK channel. By using yeast two-hybrid assays and co-immunoprecipitations from transfected cells, we demonstrate that Golgin-160 associates with the ROMK C-terminus. Immunofluorescence microscopy confirmed that both proteins are co-localized in the Golgi region. The interaction was further confirmed by the enhancement of ROMK currents by the co-expressed Golgin-160 in Xenopus oocytes. The increase in ROMK current amplitude was due to an increase in cell surface density of ROMK protein. Golgin-160 also stimulated current amplitudes of the related Kir2.1, and of voltage-gated Kv1.5 and Kv4.3 channels, but not the current amplitude of co-expressed HERG channel. These results demonstrate that the Golgi-associated Golgin-160 recognizes the cytoplasmic C-terminus of ROMK, thereby facilitating the transport of ROMK to the cell surface. However, the stimulatory effect on the activity of more distantly-related potassium channels suggests a more general role of Golgin-160 in the trafficking of plasma membrane proteins.
AB - The weak inward rectifier potassium channel ROMK is important for water and salt reabsorption in the kidney. Here we identified Golgin-160 as a novel interacting partner of the ROMK channel. By using yeast two-hybrid assays and co-immunoprecipitations from transfected cells, we demonstrate that Golgin-160 associates with the ROMK C-terminus. Immunofluorescence microscopy confirmed that both proteins are co-localized in the Golgi region. The interaction was further confirmed by the enhancement of ROMK currents by the co-expressed Golgin-160 in Xenopus oocytes. The increase in ROMK current amplitude was due to an increase in cell surface density of ROMK protein. Golgin-160 also stimulated current amplitudes of the related Kir2.1, and of voltage-gated Kv1.5 and Kv4.3 channels, but not the current amplitude of co-expressed HERG channel. These results demonstrate that the Golgi-associated Golgin-160 recognizes the cytoplasmic C-terminus of ROMK, thereby facilitating the transport of ROMK to the cell surface. However, the stimulatory effect on the activity of more distantly-related potassium channels suggests a more general role of Golgin-160 in the trafficking of plasma membrane proteins.
KW - Amino Acid Sequence
KW - Animals
KW - Autoantigens/genetics
KW - Binding Sites
KW - Biological Transport, Active
KW - COS Cells
KW - Cell Line
KW - Chlorocebus aethiops
KW - Female
KW - Gene Library
KW - Golgi Matrix Proteins
KW - Humans
KW - In Vitro Techniques
KW - Kidney/metabolism
KW - Membrane Proteins/genetics
KW - Molecular Sequence Data
KW - Multiprotein Complexes
KW - Oocytes/metabolism
KW - Potassium Channels, Inwardly Rectifying/chemistry
KW - Rats
KW - Recombinant Proteins/chemistry
KW - Two-Hybrid System Techniques
KW - Xenopus laevis
U2 - 10.1159/000091454
DO - 10.1159/000091454
M3 - SCORING: Journal article
C2 - 16543716
VL - 17
SP - 1
EP - 12
JO - CELL PHYSIOL BIOCHEM
JF - CELL PHYSIOL BIOCHEM
SN - 1015-8987
IS - 1-2
ER -
