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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2003-5-23
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pubmed:abstractText |
Plasma membrane Ca(2+) ATPases (PMCAs) maintain intracellular Ca(2+) homeostasis and participate in the local regulation of Ca(2+) signaling. Spatially separate demands for Ca(2+) regulation require proper membrane targeting of PMCAs, but the mechanism of PMCA targeting is unknown. Using the PMCA2b carboxyl-terminal tail as yeast two-hybrid bait, we isolated a novel PDZ domain-containing protein from a human brain cDNA library. This protein, named PISP for PMCA-interacting single-PDZ protein, consists of 140 amino acids and contains little else besides a single PDZ domain. Pulldown experiments showed that PISP interacts with all PMCA b-splice forms. PISP was found to be ubiquitously expressed and, in MDCK cells, was present in a punctate pattern throughout the cytosol and at the basolateral membrane. When added to microsomal membranes expressing PMCA4b, PISP was unable to stimulate the PMCA-dependent ATPase activity. Our data suggest that PISP is a transiently interacting partner of the PMCA b-splice forms that may play a role in their sorting to or from the plasma membrane.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0077-8923
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
986
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
461-71
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12763866-Alternative Splicing,
pubmed-meshheading:12763866-Amino Acid Sequence,
pubmed-meshheading:12763866-Animals,
pubmed-meshheading:12763866-Binding Sites,
pubmed-meshheading:12763866-Brain,
pubmed-meshheading:12763866-Calcium-Transporting ATPases,
pubmed-meshheading:12763866-Carrier Proteins,
pubmed-meshheading:12763866-Cation Transport Proteins,
pubmed-meshheading:12763866-Cell Line,
pubmed-meshheading:12763866-Cell Membrane,
pubmed-meshheading:12763866-Cloning, Molecular,
pubmed-meshheading:12763866-Dogs,
pubmed-meshheading:12763866-Exons,
pubmed-meshheading:12763866-Gene Library,
pubmed-meshheading:12763866-Genetic Variation,
pubmed-meshheading:12763866-Humans,
pubmed-meshheading:12763866-Introns,
pubmed-meshheading:12763866-Membrane Proteins,
pubmed-meshheading:12763866-Molecular Sequence Data,
pubmed-meshheading:12763866-Plasma Membrane Calcium-Transporting ATPases,
pubmed-meshheading:12763866-Sequence Alignment,
pubmed-meshheading:12763866-Sequence Homology, Amino Acid,
pubmed-meshheading:12763866-Transfection
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pubmed:year |
2003
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pubmed:articleTitle |
Characterization of PISP, a novel single-PDZ protein that binds to all plasma membrane Ca2+-ATPase b-splice variants.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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