SLC17A7 encodes a multifunctional transporter critical for glutamatergic neurotransmission. At synaptic vesicles in excitatory neurons, it functions primarily as a uniporter that accumulates L-glutamate from the cytoplasm into vesicles, driven by the proton electrochemical gradient established by the vacuolar H+-ATPase. The protein also exhibits chloride channel activity and K+/H+ antiport capacity, both of which modulate the vesicular proton gradient and support sustained glutamate loading. At the plasma membrane following exocytosis, SLC17A7 functions as a sodium-phosphate symporter, regulating synaptic phosphate homeostasis. The transporter is necessary for visual-evoked responses from photoreceptors. Disruption of SLC17A7 function is implicated in multiple neuropsychiatric and neurological conditions. In Alzheimer's disease, SLC17A7 is identified as a hub gene associated with early synaptic abnormalities 1, and polymorphisms in SLC17A7 show association with negative symptoms in schizophrenia 2. In glioblastoma, SLC17A7 is characterized as a bivalent tumor suppressor gene that is downregulated in glioma stem cells and inhibits tumor cell proliferation, migration, and invasion 3. Recent work identifies SLC17A7 as a consistently downregulated hub gene in glioma with strong diagnostic potential 4. Additionally, SLC17A7 is identified as a potential hub gene in HIV encephalitis 5 and in ADHD-associated brain structure alterations 6. The emerging role of specialized astrocytes in glutamatergic signaling involves VGLUT1 (SLC17A7), with subpopulation-specific deletion revealing contributions to cortico-hippocampal and nigrostriatal circuits 7.