Solute carrier family 12 member 4 (also known as KCC1) is a chloride potassium symporter. Most K-Cl cotransport in the erythrocyte is attributed to KCC1. KCC1 activity is volume-, pH-, and chloride-dependent. The regulating mechanisms include cell volume, pH, PO2, magnesium, calcium, and oxidative changes. Another regulatory pathway of KCC1 activity is a phosphorylation/ dephosphorylation cycle with phosphorylation of the transporter or a regulatory protein decreasing KCC activity and dephosphorylation increasing activity.
|Basic Information of SLC12A4|
|Protein Name||Solute carrier family 12 member 4|
|Aliases||Electroneutral potassium-chloride cotransporter 1, Erythroid K-Cl cotransporter 1(hKCC1)|
|Organism||Homo sapiens (Human)|
Solute carrier family 12 member 4 (SLC12A4) can mediate electroneutral potassium-chloride cotransport when it is activated by cell swelling. It may help to cell volume homeostasis in single cells and also be involved in the regulation of basolateral Cl- exit in NaCl absorbing epithelia. It is different from other isoforms, SLC12A4 has no transport activity. Moreover, it also influences cation-coupled chloride cotransporters in human.
Fig.1 Two astrocytic subpopulations differing in the gene expression levels of K+/Cl− channels. (Jana, 2012)
The authors show us the importance of the N- and C-terminal cytoplasmic domains to its K-Cl cotransport function expressed in Xenopus oocytes. They conclude that C-terminal loss-of-function mutants lack a dominant negative phenotype.
This article shows us that IGF-II can boost KCC1 gene expression in cervical cancer cells through the ERK1/2MAPK and PI3K/AKT signal transduction pathways.
In this article, authors find that the intron 1 (AC) repeat in CAST/Ei and SPRET/Ei is not only more divergent in length but also underwent additional sequence variation. An intron 17 B1 Alu-like SINE present in all musculus strains is found to be absent from intron 17 in SPRET/Ei.
This article finds that a single mutant allele of Kcc1 is able to induce widespread sickling and tissue damage. It provides in vivo evidence that increasing KCC activity worsens end-organ damage and diminishes survival in sickle cell disease.
The article shows that Kcc1 cross-linking is time-dependent and is independent of protein concentration. Kcc1 cross-linking by the cleavable cross-linker DTME is reversible. They support the oligomeric state of KCC polypeptides.
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