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Title:
Intracellular Pathways of Copper Trafficking in Yeast and Humans | SpringerLink
Description:
In the bakers yeast S. cerevisiae, there at least four intracellular targets requiring copper ions- 1) Ccc2p and Fet3p in the secretory pathway (homologues to Menkes/Wilson proteins and ceruloplasmin); 2) cytochrome oxidase in the mitochondria; 3) copper...
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(1985) Is hydroxyl radical generated by the fenton reaction in vivo?

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ScholarlyArticle:
      headline:Intracellular Pathways of Copper Trafficking in Yeast and Humans
      pageEnd:254
      pageStart:247
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-4615-4859-1.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Copper Transport and Its Disorders
         isbn:
            978-1-4615-4859-1
            978-1-4613-7204-2
         type:Book
      publisher:
         name:Springer US
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Valeria Cizewski Culotta
            affiliation:
                  name:Johns Hopkins University School of Public Health
                  address:
                     name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Su-Ju Lin
            affiliation:
                  name:Johns Hopkins University School of Public Health
                  address:
                     name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Paul Schmidt
            affiliation:
                  name:Johns Hopkins University School of Public Health
                  address:
                     name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Leo W. J. Klomp
            affiliation:
                  name:Washington University School of Medicine
                  address:
                     name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Ruby Leah B. Casareno
            affiliation:
                  name:Washington University School of Medicine
                  address:
                     name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Jonathan Gitlin
            affiliation:
                  name:Washington University School of Medicine
                  address:
                     name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Amyotrophic Lateral Sclerosis, Cytochrome Oxidase, Secretory Pathway, Wilson Disease, Familial Amyotrophic Lateral Sclerosis
      description:In the bakers yeast S. cerevisiae, there at least four intracellular targets requiring copper ions- 1) Ccc2p and Fet3p in the secretory pathway (homologues to Menkes/Wilson proteins and ceruloplasmin); 2) cytochrome oxidase in the mitochondria; 3) copper transcription factors in the nucleus; and 4) Cu/Zn Superoxide dismutase (SOD1) in the cytosol. We have discovered a small soluble copper carrier that specifically delivers copper ions to the secretory pathway. This 8.2 kDa factor known as Atxlp, exhibits striking homology to the MERp mercury carrier of bacteria and contains a single MTCXXC metal binding site also found in the Menkes/Wilson family of copper transporting ATPases. Our studies show that Atxlp is cytosolic and facilitates the delivery of copper ions from the cell surface copper transporter to Ccc2p and Fet3p in the secretory pathway; furthermore, it is not involved in the delivery of copper ions to the mitochondria, the nucleus or cytosolic SOD1, implicating specific signals directing Atx 1p to the secretory pathway. Homologues to Atx 1p have been found in invertebrates, plants and humans, and the human gene is abundantly expressed in all tissues. In addition to Atx 1p, we have recently uncovered an additional metal trafficking protein that appears to specifically deliver copper ions to SOD1. Mutants in the corresponding gene (lys 7) are defective for SOD1 activity, and are unable to incorporate copper into SOD1, while there is no obvious impairment in copper delivery to cytochrome oxidase or Fet3p. The encoded 27 kDa protein contains a single MHCXXC consensus copper binding sequence and close homologues have been identified in a wide array of eukaryotic species including humans.
      datePublished:1999
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Book:
      name:Copper Transport and Its Disorders
      isbn:
         978-1-4615-4859-1
         978-1-4613-7204-2
Organization:
      name:Springer US
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Johns Hopkins University School of Public Health
      address:
         name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
         type:PostalAddress
      name:Johns Hopkins University School of Public Health
      address:
         name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
         type:PostalAddress
      name:Johns Hopkins University School of Public Health
      address:
         name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
         type:PostalAddress
      name:Washington University School of Medicine
      address:
         name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
         type:PostalAddress
      name:Washington University School of Medicine
      address:
         name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
         type:PostalAddress
      name:Washington University School of Medicine
      address:
         name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Valeria Cizewski Culotta
      affiliation:
            name:Johns Hopkins University School of Public Health
            address:
               name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
               type:PostalAddress
            type:Organization
      name:Su-Ju Lin
      affiliation:
            name:Johns Hopkins University School of Public Health
            address:
               name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
               type:PostalAddress
            type:Organization
      name:Paul Schmidt
      affiliation:
            name:Johns Hopkins University School of Public Health
            address:
               name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
               type:PostalAddress
            type:Organization
      name:Leo W. J. Klomp
      affiliation:
            name:Washington University School of Medicine
            address:
               name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
               type:PostalAddress
            type:Organization
      name:Ruby Leah B. Casareno
      affiliation:
            name:Washington University School of Medicine
            address:
               name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
               type:PostalAddress
            type:Organization
      name:Jonathan Gitlin
      affiliation:
            name:Washington University School of Medicine
            address:
               name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
      name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
      name:Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, USA
      name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
      name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
      name:Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, USA
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