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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-2-22
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pubmed:databankReference |
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pubmed:abstractText |
Ca2+-binding proteins containing EF-hands are important constituents of intracellular signaling pathways. Recently, three new members of the Neuronal Calcium Sensor subgroup have been cloned in humans. Calsenilin interacts with presenilins, DREAM is a calcium-regulated transcriptional repressor and KChIP3 binds and modulates A-type potassium channels. Here we describe the mouse full-length cDNA and the genomic locus, demonstrating that the three proteins are encoded by the same unique gene. Various mechanisms contribute to the coding potential of this locus. These include alternate translation starts in the first exon and alternative splicing yielding transcripts lacking the EF-hand domains. In situ hybridization, RT-PCR, and Northern blotting reveal nervous system-restricted expression largely coinciding with the distribution of the Kv4.2 alpha-subunit of potassium channels. The presence of transcripts in early embryonic stages suggests roles for the protein also during development.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Codon, Initiator,
http://linkedlifedata.com/resource/pubmed/chemical/Csen protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Kv Channel-Interacting Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Shal Potassium Channels
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1044-7431
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-16
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:11161465-Alternative Splicing,
pubmed-meshheading:11161465-Amino Acid Sequence,
pubmed-meshheading:11161465-Animals,
pubmed-meshheading:11161465-Base Sequence,
pubmed-meshheading:11161465-Blotting, Northern,
pubmed-meshheading:11161465-Calcium-Binding Proteins,
pubmed-meshheading:11161465-Central Nervous System,
pubmed-meshheading:11161465-Cloning, Molecular,
pubmed-meshheading:11161465-Codon, Initiator,
pubmed-meshheading:11161465-DNA, Complementary,
pubmed-meshheading:11161465-Exons,
pubmed-meshheading:11161465-In Situ Hybridization,
pubmed-meshheading:11161465-Kv Channel-Interacting Proteins,
pubmed-meshheading:11161465-Mice,
pubmed-meshheading:11161465-Mice, Inbred C57BL,
pubmed-meshheading:11161465-Molecular Sequence Data,
pubmed-meshheading:11161465-Organ Specificity,
pubmed-meshheading:11161465-Potassium Channels,
pubmed-meshheading:11161465-Potassium Channels, Voltage-Gated,
pubmed-meshheading:11161465-Protein Structure, Tertiary,
pubmed-meshheading:11161465-RNA, Messenger,
pubmed-meshheading:11161465-Repressor Proteins,
pubmed-meshheading:11161465-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11161465-Shal Potassium Channels
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pubmed:year |
2001
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pubmed:articleTitle |
Mouse DREAM/calsenilin/KChIP3: gene structure, coding potential, and expression.
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pubmed:affiliation |
Max-Planck-Institute of Neurobiology, Am Klopferspitz 18A, Martinsried, D-82152, Germany.
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pubmed:publicationType |
Journal Article
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