Journal
JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY
Volume 57, Issue -, Pages 68-71Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.yjmcc.2013.01.010
Keywords
Na+/Ca2+ exchange; Membrane proteins; Topology; Crosslinking
Categories
Funding
- National Institutes of Health [HL49101]
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The topology of the plasma membrane Na+/Ca2+ exchanger of cardiac muscle, NCX1, is uncertain. Biochemical analyses have indicated the presence of 9 transmembrane segments (TMSs) whereas the recent crystal structure of a prokaryotic homologue has 10 TMSs. The discrepancy is towards the C-terminus of the proteins where the prokaryotic homologue has an additional TMS8. To resolve this apparent disagreement, we re-assessed the topology of the C-terminal TMSs of NCX1. We examined the ability of internal or external cysteine residues in the N-terminal portion of NCX1 to crosslink with cysteine residues, of uncertain orientation, in the C-terminal portion of the protein. The results strongly support a model of NCX1 with 10 TMSs as found in the prokaryotic homologue. (C) 2013 Elsevier Ltd. All rights reserved.
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