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Differential Protein Mobility of the -Aminobutyric Acid, Type A, Receptor and Subunit Channel-lining Segments*
 

Summary: Differential Protein Mobility of the -Aminobutyric Acid, Type A,
Receptor and Subunit Channel-lining Segments*
Received for publication, September 21, 2004, and in revised form, October 29, 2004
Published, JBC Papers in Press, November 2, 2004, DOI 10.1074/jbc.M410881200
Jeffrey Horenstein, Paul Riegelhaupt, and Myles H. Akabas
From the Departments of Physiology and Biophysics and of Neuroscience, Albert Einstein College of Medicine,
Yeshiva University, Bronx, New York 10461
The -aminobutyric acid, type A (GABAA), receptor
ion channel is lined by the second membrane-spanning
(M2) segments from each of five homologous subunits
that assemble to form the receptor. Gating presumably
involves movement of the M2 segments. We assayed
protein mobility near the M2 segment extracellular
ends by measuring the ability of engineered cysteines
to form disulfide bonds and high affinity Zn2
-binding
sites. Disulfide bonds formed in 1 1E270C 2 but not in
1N275C 1 2 or 1 1 2K285C. Diazepam potentiation
and Zn2
inhibition demonstrated that expressed re-

  

Source: Akabas, Myles - Department of Physiology and Biophysics, Albert Einstein College of Medicine, Yeshiva University

 

Collections: Biology and Medicine