help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 71: 749-758 (1996)
© 1996 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ferrer-Montiel, A V
Right arrow Articles by Montal, M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ferrer-Montiel, A V
Right arrow Articles by Montal, M

A single tryptophan on M2 of glutamate receptor channels confers high permeability to divalent cations.

A V Ferrer-Montiel, W Sun and M Montal

Department of Biology, University of California San Diego, La Jolla 92093-0366, USA.

ABSTRACT

Ionotropic glutamate receptors (iGluRs) of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate/kainate subtype display lower permeability to Ca2+ than the N-methyl-D-aspartate (NMDA) subtype. The well-documented N/Q/R site on the M2 transmembrane segment (M2) is an important determinant of the distinct Ca2+ permeability exhibited by members of the non-NMDA receptor subfamily. This site, however, does not completely account for the different permeation properties displayed by non-NMDA and NMDA receptors, suggesting the involvement of other molecular determinants. We have identified additional molecular elements on M2 of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate/kainate receptor GluR1 that specify its permeation properties. Higher permeability to divalent over monovalent cations is conferred on GluR1 by a tryptophan at position 577, whereas blockade by external divalent cations is imparted by an asparagine at position 582. Hence, the permeation properties of ionotropic glutamate receptors appear to be primarily specified by two distinct determinants on M2, the well-known N/Q/R site and the newly identified L/W site. These findings substantiate the notion that M2 is a structural component of the pore lining.




This article has been cited by other articles:


Home page
 J. Neurosci.Home page
F. M. Inglis, R. Crockett, S. Korada, W. C. Abraham, M. Hollmann, and R. G. Kalb
The AMPA Receptor Subunit GluR1 Regulates Dendritic Architecture of Motor Neurons
J. Neurosci., September 15, 2002; 22(18): 8042 - 8051.
[Abstract] [Full Text] [PDF]

Home page
 Pharmacol. Rev.Home page
R. Dingledine, K. Borges, D. Bowie, and S. F. Traynelis
The Glutamate Receptor Ion Channels
Pharmacol. Rev., March 1, 1999; 51(1): 7 - 62.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
K. Williams, A. J. Pahk, K. Kashiwagi, T. Masuko, N. D. Nguyen, and K. Igarashi
The Selectivity Filter of the N-Methyl-D-Aspartate Receptor: A Tryptophan Residue Controls Block and Permeation of Mg2+
Mol. Pharmacol., May 1, 1998; 53(5): 933 - 941.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
C. Garcia-Martinez, C. Morenilla-Palao, R. Planells-Cases, J. M. Merino, and A. Ferrer-Montiel
Identification of an Aspartic Residue in the P-loop of the Vanilloid Receptor That Modulates Pore Properties
J. Biol. Chem., October 13, 2000; 275(42): 32552 - 32558.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by the Biophysical Society.