Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Critical amino acids in the TM2 of EAAT2 are essential for membrane-bound localization, substrate binding, transporter function and anion currents.

Journal of cellular and molecular medicine - 1 Mar 2021

Mai Dongmei, Chen Rongqing, Wang Ji, Zheng Jiawei, Zhang Xiuping, Qu Shaogang

Abstract excerpt

Excitatory amino acid transporter 2 (EAAT2), the gene of which is known as solute carrier family 1 member 2 (SLC1A2), is an important membrane-bound transporter that mediates approximately 90% of the transport and clearance of l-glutamate at synapses in the central nervous system (CNS). Transmembrane domain 2 (TM2) of EAAT2 is close to hairpin loop 2 (HP2) and far away from HP1 in the inward-facing conformation....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Anions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biological Transport

Share to Cell Membrane

Share to Excitatory Amino Acid Transporter 2

Share to HeLa Cells

Share to Protein Interaction Domains and Motifs

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 33523598
DOI: 10.1111/jcmm.16212
PMCID: PMC7933967

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Critical amino acids in the TM2 of EAAT2 are essential for membrane-bound localization, substrate binding, transporter function and anion currents.PMID 33523598Read ↗

Mutations associated with epileptic encephalopathy modify EAAT2 anion channel function.Semantic proximity Read ↗

Highly conserved asparagine 82 controls the interaction of Na+ with the sodium-coupled neutral amino acid transporter SNAT2.Semantic proximity Read ↗

Glutamate transporter EAAT2: regulation, function, and potential as a therapeutic target for neurological and psychiatric diseaseSemantic proximity Read ↗

An amino-terminal point mutation increases EAAT2 anion currents without affecting glutamate transport ratesSemantic proximity Read ↗

Mutations in transmembrane domains 5 and 7 of the human excitatory amino acid transporter 1 affect the substrate-activated anion channel.Semantic proximity Read ↗

The role of excitatory amino acid transporter 2 (EAAT2) in epilepsy and other neurological disordersSemantic proximity Read ↗

Trafficking of the glutamate transporter is impaired in LRRK2-related Parkinson’s diseaseSemantic proximity Read ↗

Structural bioinformatics studies of glutamate transporters and their AlphaFold2 predicted water-soluble QTY variants and uncovering the natural mutations of L->Q, I->T, F->Y and Q->L, T->I and Y->F.Semantic proximity Read ↗

Trafficking of the glutamate transporter is impaired in LRRK2-related Parkinson's disease.Semantic proximity Read ↗

Molecular determinants of transport stimulation of EAAT2 are located at interface between the trimerization and substrate transport domains.Semantic proximity Read ↗

A conserved Na(+) binding site of the sodium-coupled neutral amino acid transporter 2 (SNAT2).Semantic proximity Read ↗

Two di-leucine motifs regulate trafficking and function of mouse ASIC2a.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.