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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2002-4-17
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pubmed:databankReference |
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pubmed:abstractText |
Polycystin-L (PCL) shares high homology with polycystin-2, the product of polycystic kidney disease gene-2. It was previously shown that the PCL forms a non-selective cation channel activated by calcium influx. However, it remains unclear whether calcium activates/inactivates PCL by binding to the EF-hand motif located on the cytoplasmic carboxyl-terminus. Here we obtained two PCL splice variants from liver (PCL-LV, lacking the EF-hand) and testis (PCL-TS, lacking 45 amino acids on the carboxyl tail) using PCR-based approaches. When expressed in Xenopus oocytes and studied using electrophysiology both splice variants exhibited basal cation channel activity and calcium-induced channel activation. While PCL-TS displayed similar activation to PCL, PCL-LV exhibited a three-fold increased activation. All five PCL C-terminal artificial truncation mutants also exhibited basal and calcium-activated channel activities, in particular the mutant T622X lacking the EF-hand was associated with increased activation. Our data demonstrate that the EF-hand and other parts of the carboxyl tail of PCL are not determinants of channel activation/inactivation although the EF-hand seems to be involved in the modulation of these processes.
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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 Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PKD2L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRPP Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/polycystic kidney disease 2 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
516
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
270-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11959145-Alternative Splicing,
pubmed-meshheading:11959145-Amino Acid Sequence,
pubmed-meshheading:11959145-Animals,
pubmed-meshheading:11959145-Base Sequence,
pubmed-meshheading:11959145-Binding Sites,
pubmed-meshheading:11959145-Calcium Channels,
pubmed-meshheading:11959145-Cloning, Molecular,
pubmed-meshheading:11959145-Female,
pubmed-meshheading:11959145-Humans,
pubmed-meshheading:11959145-Ion Channels,
pubmed-meshheading:11959145-Male,
pubmed-meshheading:11959145-Membrane Glycoproteins,
pubmed-meshheading:11959145-Membrane Proteins,
pubmed-meshheading:11959145-Molecular Sequence Data,
pubmed-meshheading:11959145-Mutation,
pubmed-meshheading:11959145-Oocytes,
pubmed-meshheading:11959145-Phosphoproteins,
pubmed-meshheading:11959145-Polycystic Kidney, Autosomal Dominant,
pubmed-meshheading:11959145-Protein Structure, Tertiary,
pubmed-meshheading:11959145-Receptors, Cell Surface,
pubmed-meshheading:11959145-Recombinant Proteins,
pubmed-meshheading:11959145-Sequence Deletion,
pubmed-meshheading:11959145-Sequence Homology, Amino Acid,
pubmed-meshheading:11959145-TRPP Cation Channels,
pubmed-meshheading:11959145-Xenopus
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pubmed:year |
2002
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pubmed:articleTitle |
The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation.
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pubmed:affiliation |
Department of Physiology, University of Alberta, 729 MSB, T6G 2H7, Edmonton, AB, Canada.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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