NMDA receptor channel gating control by the pre-M1 helix.

Tytuł:: NMDA receptor channel gating control by the pre-M1 helix.
Autorzy:: McDaniel MJ; Department of Pharmacology, Rollins Research Center, Emory University, Atlanta, GA.
Ogden KK; Department of Pharmacology, Rollins Research Center, Emory University, Atlanta, GA.
Kell SA; Department of Pharmacology, Rollins Research Center, Emory University, Atlanta, GA.; Department of Chemistry, Emory University, Atlanta, GA.
Burger PB; Department of Chemistry, Emory University, Atlanta, GA.
Liotta DC; Department of Chemistry, Emory University, Atlanta, GA.
Traynelis SF; Department of Pharmacology, Rollins Research Center, Emory University, Atlanta, GA.
Źródło:: The Journal of general physiology [J Gen Physiol] 2020 Apr 06; Vol. 152 (4).
Typ publikacji:: Journal Article; Research Support, N.I.H., Extramural
Język:: English
Imprint Name(s):: Publication: New York, N.Y. : Rockefeller University Press
Original Publication: New York, N.Y. : Rockefeller Institute for Medical Research, c1918-
MeSH Terms:: Ion Channel Gating/*physiology
Receptors, N-Methyl-D-Aspartate/*metabolism
Amino Acid Sequence ; Amino Acids/metabolism ; Animals ; Binding Sites/physiology ; Cell Line ; HEK293 Cells ; Humans ; Protein Domains/physiology ; Protein Subunits/metabolism ; Xenopus
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Grant Information:: F31 NS106896 United States NS NINDS NIH HHS; R01 NS036654 United States NS NINDS NIH HHS; R35 NS111619 United States NS NINDS NIH HHS; T32 GM008602 United States GM NIGMS NIH HHS
Substance Nomenclature:: 0 (Amino Acids)
0 (Protein Subunits)
0 (Receptors, N-Methyl-D-Aspartate)
Entry Date(s):: Date Created: 20200330 Date Completed: 20210608 Latest Revision: 20210608
Update Code:: 20240105
PubMed Central ID:: PMC7141592
DOI:: 10.1085/jgp.201912362
PMID:: 32221541
: Czasopismo naukowe

The NMDA receptor (NMDAR) is an ionotropic glutamate receptor formed from the tetrameric assembly of GluN1 and GluN2 subunits. Within the flexible linker between the agonist binding domain (ABD) and the M1 helix of the pore-forming transmembrane helical bundle lies a two-turn, extracellular pre-M1 helix positioned parallel to the plasma membrane and in van der Waals contact with the M3 helix thought to constitute the channel gate. The pre-M1 helix is tethered to the bilobed ABD, where agonist-induced conformational changes initiate activation. Additionally, it is a locus for de novo mutations associated with neurological disorders, is near other disease-associated de novo sites within the transmembrane domain, and is a structural determinant of subunit-selective modulators. To investigate the role of the pre-M1 helix in channel gating, we performed scanning mutagenesis across the GluN2A pre-M1 helix and recorded whole-cell macroscopic and single channel currents from HEK293 cell-attached patches. We identified two residues at which mutations perturb channel open probability, the mean open time, and the glutamate deactivation time course. We identified a subunit-specific network of aromatic amino acids located in and around the GluN2A pre-M1 helix to be important for gating. Based on these results, we are able to hypothesize about the role of the pre-M1 helix in other NMDAR subunits based on sequence and structure homology. Our results emphasize the role of the pre-M1 helix in channel gating, implicate the surrounding amino acid environment in this mechanism, and suggest unique subunit-specific contributions of pre-M1 helices to GluN1 and GluN2 gating.
(© 2020 McDaniel et al.)

Comment in: J Gen Physiol. 2020 Apr 6;152(4):. (PMID: 32221542)

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