Solute carrier family 9A7 (SLC9A7) is also known as sodium/hydrogen exchanger 7 or sodium-hydrogen antiporter 7 (NHE-7). It is encoded by the SLC9A7 gene in humans. SLC9A7 is broadly expressed in the brain, lymph node, and 24 other tissues. The SLC9A7 gene is conserved in Rhesus monkey, chicken, chimpanzee, dog, zebrafish, mouse, cow, zebrafish, and frog. It belongs to the solute carrier family 9, and functions as a Na+/H+ antiporter. The most well-known function of SLC9A7 is to involve in pH homeostasis, and signal transduction.
|Basic Information of SLC9A7|
|Protein Name||Sodium/hydrogen exchanger 7|
|Aliases||Na(+)/H(+) exchanger 7, NHE7|
|Organism||Homo sapiens (Human)|
As a member of SLC9A family, SLC9A7 mediates the sodium-ion transport and plays an important role in cell pH regulation and cell volume. SLC9A7 is associated with Nef internalization into M2 macrophages. In addition, SLC9A7 is localized to the Golgi network and is associated with pH homeostasis via endocytic and secretory pathways. Moreover, SLC9A7 has a functional role in the development of breast tumors via promoting cell growth, cell adhesion, and invasion. SLC9A7 is associated with sodium-coupled proton loading mechanism in endocytosis. SLC9A7 plays potential dual roles in intracellular compartments, and also indicates the characteristics of subdomains of cell-surface membranes. Furthermore, the trafficking of SLC9A7 can be regulated by secretory carrier membrane proteins.
Fig.1 Topology of SLC9A7.
This article indicates that SLC9A7 is associated with sodium-coupled proton loading mechanism in endocytosis.
This article reveals NHE7’s functions in oncogenic processes. NHE7 can modulate cell adhesion, invasion and anchorage-independent growth of breast cancer.
This article indicates that the specific regions of NHE7 are critical for NHE7 localization mechanism in the trans-Golgi network which is different from NHE6.
This article shows that NHE7 plays potential dual roles in intracellular compartments, and also indicates the characteristics of subdomains of cell-surface membranes.
This article shows the novel mechanism of caveolins binding to NHE7. The caveolins include caveolae/lipid rafts and non-caveolae/lipid raft which display different dynamics.
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