Intermolecular cross-linking of na(+)-ca(2+) exchanger proteins: evidence for dimer formation.

Intermolecular cross-linking of na(+)-ca(2+) exchanger proteins: evidence for dimer formation. Research Abstract Details 

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Intermolecular cross-linking of na(+)-ca(2+) exchanger proteins: evidence for dimer formation. Abstract Text:

The cardiac Na (+)-Ca (2+) exchanger (NCX1) is modeled to contain nine transmembrane segments (TMS) with a pair of oppositely oriented, conserved sequences called the alpha-repeats that are important in ion transport. Residue 122 in the alpha-1 repeat is in proximity to residue 768 in TMS 6, and the two residues can be cross-linked . During studies on the substrate specificity of this intramolecular cross-link, we found evidence that NCX1 can form dimers. At 37 degrees C in the absence of extracellular Na (+), copper phenanthroline catalyzes disulfide bond formation between cysteines at position 122 in adjacent NCX1 proteins. Dimerization was confirmed by histidine tag pull-down experiments that demonstrate the association of untagged NCX1 with histidine-tagged NCX1. Dimerization occurs along a face of the protein that includes parts of the alpha-1 and alpha-2 repeats as well as parts of TMS 1 and TMS 2. We do not see cross-linking between residues in TMS 5, TMS 6, or TMS 7. These data provide the first evidence for dimer formation by the Na (+)-Ca (2+) exchanger.

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Intermolecular cross-linking of na(+)-ca(2+) exchanger proteins: evidence for dimer formation. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biochemistry

VOLUME: 47

Page Numbers: 6081-7

Journal Abbreviation: Biochemistry

ISSN: 1520-4995

DAY: 9

MONTH: 05

YEAR: 2008

Intermolecular cross-linking of na(+)-ca(2+) exchanger proteins: evidence for dimer formation. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Intermolecular cross-linking of na(+)-ca(2+) exchanger proteins: evidence for dimer formation.

AFFILIATION: KPhilipson@mednet.ucla.edu.

Country: United States

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MEDLINETA: Biochemistry

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