Source:http://linkedlifedata.com/resource/pubmed/id/14726528
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
2004-3-29
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pubmed:abstractText |
The neuronal calcium sensor (NCS) family of Ca(2+)-binding proteins regulates a number of different processes in neurons and photoreceptor cells. The first of these proteins to be characterized, recoverin, was shown to exhibit a Ca(2+)/myristoyl switch whereby its N-terminal myristoyl group is sequestered in the Ca(2+)-free form and is exposed on Ca(2+) binding to allow the protein to become membrane-associated. It has subsequently been shown that certain other family members also exhibit this mechanism in living cells. In contrast, NCS-1 does not show the Ca(2+)/myristoyl switch and is membrane-associated even at low Ca(2+) concentrations. We have used sequence comparison combined with information from structural analyses to attempt to identify candidate residues within the NCS proteins that determine whether or not the Ca(2+)/myristoyl switch operates in cells and have tested their functional significance by mutagenesis. The results show that NCS-1 possesses residues within its N terminus that lock the myristoyl group in an exposed conformation. In addition, other structural aspects within the C-terminal domains are required to allow the switch to operate. We have determined a key role for residues within the motif EELTRK in NCS-1 in keeping the myristoyl group exposed and allowing the protein to be constitutively membrane-associated.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hippocalcin,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
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/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/frequenin calcium sensor proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14347-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14726528-Amino Acid Sequence,
pubmed-meshheading:14726528-Calcium,
pubmed-meshheading:14726528-Calcium-Binding Proteins,
pubmed-meshheading:14726528-HeLa Cells,
pubmed-meshheading:14726528-Hippocalcin,
pubmed-meshheading:14726528-Humans,
pubmed-meshheading:14726528-Molecular Sequence Data,
pubmed-meshheading:14726528-Myristic Acid,
pubmed-meshheading:14726528-Nerve Tissue Proteins,
pubmed-meshheading:14726528-Neuronal Calcium-Sensor Proteins,
pubmed-meshheading:14726528-Neurons,
pubmed-meshheading:14726528-Neuropeptides,
pubmed-meshheading:14726528-Protein Structure, Tertiary,
pubmed-meshheading:14726528-Recombinant Fusion Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Identification of residues that determine the absence of a Ca(2+)/myristoyl switch in neuronal calcium sensor-1.
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pubmed:affiliation |
Physiological Laboratory, University of Liverpool, Crown Street, Liverpool L69 3BX, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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