The CCC2 gene in the yeastSaccharomyces cerevisiae encodes a P-type ATPase (Ccc2p) required for the export of cytosolic copper to the extracytosolic domain of a copper-dependent oxidase, Fet3p. Ccc2p appears to be both a structural and functional homolog of ATPases impaired in two human disorders of intracellular copper transport, Menkes disease and Wilson disease. In the present work, three approaches were used to determine the locus of Ccc2p-dependent copper export within the secretory pathway. First, like ccc2 mutants,sec mutants blocked in the secretory pathway at steps prior to and including the Golgi complex failed to deliver radioactive copper to Fet3p. Second, also like ccc2 mutants, vps33and certain other mutants with defects in post-Golgi sorting exhibited phenotypes traceable to deficient copper delivery to Fet3p. These findings were sufficient to explain the respiratory deficiency of these mutants. Third, immunofluorescence microscopy revealed that Ccc2p was distributed among several punctate foci within wild-type cells, consistent with late Golgi or post-Golgi localization. Thus, copper export by Ccc2p appears to be restricted to a late or post-Golgi compartment in the secretory pathway.
Restriction of Copper Export in Saccharomyces cerevisiae to a Late Golgi or Post-Golgi Compartment in the Secretory Pathway*
Published 1997 in Journal of Biological Chemistry
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- Publication year
1997
- Venue
Journal of Biological Chemistry
- Publication date
1997-10-10
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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