University of Montana ScholarWorks at University of Montana Biomedical and Pharmaceutical Sciences Faculty Biomedical and Pharmaceutical Sciences Publications 1997 Tyrosine 140 of the γ-Aminobutyric Acid Transporter GAT-1 Plays a Critical Role in Neurotransmitter Recognition Yona Bismuth Michael Kavanaugh University of Montana - Missoula Baruch I. Kanner Let us know how access to this document benefits ouy . Follow this and additional works at: https://scholarworks.umt.edu/biopharm_pubs Part of the Medical Sciences Commons, and the Pharmacy and Pharmaceutical Sciences Commons Recommended Citation Bismuth, Yona; Kavanaugh, Michael; and Kanner, Baruch I., "Tyrosine 140 of the γ-Aminobutyric Acid Transporter GAT-1 Plays a Critical Role in Neurotransmitter Recognition" (1997). Biomedical and Pharmaceutical Sciences Faculty Publications. 58. https://scholarworks.umt.edu/biopharm_pubs/58 This Article is brought to you for free and open access by the Biomedical and Pharmaceutical Sciences at ScholarWorks at University of Montana. It has been accepted for inclusion in Biomedical and Pharmaceutical Sciences Faculty Publications by an authorized administrator of ScholarWorks at University of Montana. For more information, please contact
[email protected]. THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 272, No. 26, Issue of June 27, pp. 16096–16102, 1997 © 1997 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Tyrosine 140 of the g-Aminobutyric Acid Transporter GAT-1 Plays a Critical Role in Neurotransmitter Recognition* (Received for publication, February 6, 1997, and in revised form, April 8, 1997) Yona Bismuth‡, Michael P. Kavanaugh§, and Baruch I. Kanner‡¶ From the ‡Department of Biochemistry, Hadassah Medical School, the Hebrew University, Jerusalem 91120, Israel and the §Vollum Institute, Oregon Health Science University, Portland, Oregon 97201 The g-aminobutyric acid (GABA) transporter GAT-1 is tify amino acid residues of GAT-1 involved in substrate bind- located in nerve terminals and catalyzes the electro- ing.