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Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Commun+Biol 2021 ; 4 (1): 226 Nephropedia Template TP
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The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2 #MMPMID33597714
Zhang S; Zhou J; Zhang Y; Liu T; Friedel P; Zhuo W; Somasekharan S; Roy K; Zhang L; Liu Y; Meng X; Deng H; Zeng W; Li G; Forbush B; Yang M
Commun Biol 2021[Feb]; 4 (1): 226 PMID33597714show ga
NKCC and KCC transporters mediate coupled transport of Na(+)+K(+)+Cl(-) and K(+)+Cl(-) across the plasma membrane, thus regulating cell Cl(-) concentration and cell volume and playing critical roles in transepithelial salt and water transport and in neuronal excitability. The function of these transporters has been intensively studied, but a mechanistic understanding has awaited structural studies of the transporters. Here, we present the cryo-electron microscopy (cryo-EM) structures of the two neuronal cation-chloride cotransporters human NKCC1 (SLC12A2) and mouse KCC2 (SLC12A5), along with computational analysis and functional characterization. These structures highlight essential residues in ion transport and allow us to propose mechanisms by which phosphorylation regulates transport activity.
|Animals[MESH]
|Anions[MESH]
|Binding Sites[MESH]
|Cations[MESH]
|Cryoelectron Microscopy[MESH]
|HEK293 Cells[MESH]
|Humans[MESH]
|Ion Channel Gating[MESH]
|Ion Transport[MESH]
|K Cl- Cotransporters[MESH]
|Molecular Dynamics Simulation[MESH]
|Phosphorylation[MESH]
|Protein Binding[MESH]
|Protein Conformation[MESH]
|Sf9 Cells[MESH]
|Solute Carrier Family 12, Member 2/genetics/*metabolism/ultrastructure[MESH]