Linked Life Data

16051599

Source:http://linkedlifedata.com/resource/pubmed/id/16051599

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
2005-9-26
pubmed:abstractText
The homeostatic regulation of essential elements such as copper requires many proteins whose activities are often mediated and tightly coordinated through protein-protein interactions. This regulation ensures that cells receive enough copper without intracellular concentrations reaching toxic levels. To date, only a small number of proteins implicated in copper homeostasis have been identified, and little is known of the protein-protein interactions required for this process. To identify other proteins important for copper homeostasis, while also elucidating the protein-protein interactions that are integral to the process, we have utilized a known copper protein, the copper ATPase ATP7A, as a bait in a yeast two-hybrid screen of a human cDNA library to search for interacting partners. One of the ATP7A-interacting proteins identified is a novel protein with a single PDZ domain. This protein was recently identified to interact with the plasma membrane calcium ATPase b-splice variants. We propose a change in name for this protein from PISP (plasma membrane calcium ATPase-interacting single-PDZ protein) to AIPP1 (ATPase-interacting PDZ protein) and suggest that it represents the protein that interacts with the class I PDZ binding motif identified at the ATP7A C terminus. The interaction in mammalian cells was confirmed and an additional splice variant of AIPP1 was identified. This study represents an essential step forward in identifying the proteins and elucidating the network of protein-protein interactions involved in maintaining copper homeostasis and validates the use of the yeast two-hybrid approach for this purpose.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33270-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:16051599-Adenosine Triphosphatases, pubmed-meshheading:16051599-Alternative Splicing, pubmed-meshheading:16051599-Amino Acid Motifs, pubmed-meshheading:16051599-Amino Acid Sequence, pubmed-meshheading:16051599-Binding Sites, pubmed-meshheading:16051599-Carrier Proteins, pubmed-meshheading:16051599-Cation Transport Proteins, pubmed-meshheading:16051599-Cell Line, Transformed, pubmed-meshheading:16051599-Copper, pubmed-meshheading:16051599-Fibroblasts, pubmed-meshheading:16051599-Gene Library, pubmed-meshheading:16051599-Genetic Variation, pubmed-meshheading:16051599-Homeostasis, pubmed-meshheading:16051599-Humans, pubmed-meshheading:16051599-Menkes Kinky Hair Syndrome, pubmed-meshheading:16051599-Molecular Sequence Data, pubmed-meshheading:16051599-Mutagenesis, Site-Directed, pubmed-meshheading:16051599-Mutation, pubmed-meshheading:16051599-Precipitin Tests, pubmed-meshheading:16051599-Protein Binding, pubmed-meshheading:16051599-Protein Structure, Tertiary, pubmed-meshheading:16051599-Proteins, pubmed-meshheading:16051599-Recombinant Fusion Proteins, pubmed-meshheading:16051599-Sequence Homology, Amino Acid, pubmed-meshheading:16051599-Transcription, Genetic, pubmed-meshheading:16051599-Two-Hybrid System Techniques, pubmed-meshheading:16051599-beta-Galactosidase
pubmed:year
2005
pubmed:articleTitle
A single PDZ domain protein interacts with the Menkes copper ATPase, ATP7A. A new protein implicated in copper homeostasis.
pubmed:affiliation
Centre for Cellular and Molecular Biology, School of Biological and Chemical Sciences, Deakin University, Burwood, Victoria 3125, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't