Topologic Investigation of the NCKX2 Na + /Ca 2+ ‐K + Exchanger α‐Repeats

Algorithms suggest that NCKX proteins consist of an N‐terminal signal peptide and 11 transmembrane segments divided in two groups of 5 and 6, respectively, separated by a large cytoplasmic loop. This predicted topology places the NCKX α‐repeats with the same orientation in the plasma membrane. Using...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 2007-03, Vol.1099 (1), p.34-39
Main Authors: KINJO, TASHI G., SZERENCSEI, ROBERT T., SCHNETKAMP, PAUL P. M.
Format: Article
Language:English
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Summary:Algorithms suggest that NCKX proteins consist of an N‐terminal signal peptide and 11 transmembrane segments divided in two groups of 5 and 6, respectively, separated by a large cytoplasmic loop. This predicted topology places the NCKX α‐repeats with the same orientation in the plasma membrane. Using thiol‐specific drug treatment and site‐directed disulfide mapping, we have investigated the orientation of the NCKX2 α‐repeats. Our results suggest that the NCKX2 α‐repeats have an antiparallel orientation in the plasma membrane. In addition, these experiments suggest that the α‐repeats are found in close proximity in the mature configuration of the protein.
ISSN:0077-8923
1749-6632
DOI:10.1196/annals.1387.055