Source:http://linkedlifedata.com/resource/pubmed/id/14512421
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
49
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pubmed:dateCreated |
2003-12-3
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pubmed:abstractText |
Frequenin, also known as neuronal calcium sensor-1 (NCS-1), is an N-myristoylated Ca2+-binding protein that has been conserved in both sequence and three-dimensional fold during evolution. We demonstrate using both genetic and biochemical approaches that the observed structural conservation between Saccharomyces cerevisiae frequenin (Frq1) and human NCS-1 is also reflected at the functional level. In yeast, the sole essential target of Frq1 is the phosphatidylinositol 4-kinase isoform, Pik1; both FRQ1 and PIK1 are indispensable for cell viability. Expression of human NCS-1 in yeast, but not a close relative (human KChIP2), rescues the inviability of frq1 cells. Furthermore, in vitro, Frq1 and NCS-1 (either N-myristoylated or unmyristoylated) compete for binding to a small 28-residue motif near the N terminus of Pik1. Site-directed mutagenesis indicates that the binding determinant in Pik1 is a hydrophobic alpha-helix and that frequenins bind to one side of this alpha-helix. We propose, therefore, that the function of NCS-1 in mammals may closely resemble that of Frq1 in S. cerevisiae and, hence, that frequenins in general may serve as regulators of certain isoforms of phosphatidylinositol 4-kinase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-Phosphatidylinositol 4-Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuronal Calcium-Sensor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/PIK1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/frequenin calcium sensor proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
49589-99
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pubmed:dateRevised |
2007-12-11
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pubmed:meshHeading |
pubmed-meshheading:14512421-1-Phosphatidylinositol 4-Kinase,
pubmed-meshheading:14512421-Calcium-Binding Proteins,
pubmed-meshheading:14512421-Humans,
pubmed-meshheading:14512421-Mutagenesis, Site-Directed,
pubmed-meshheading:14512421-Nerve Tissue Proteins,
pubmed-meshheading:14512421-Neuronal Calcium-Sensor Proteins,
pubmed-meshheading:14512421-Neuropeptides,
pubmed-meshheading:14512421-Protein Binding,
pubmed-meshheading:14512421-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:14512421-Two-Hybrid System Techniques
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pubmed:year |
2003
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pubmed:articleTitle |
Conservation of regulatory function in calcium-binding proteins: human frequenin (neuronal calcium sensor-1) associates productively with yeast phosphatidylinositol 4-kinase isoform, Pik1.
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pubmed:affiliation |
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3200, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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