Source:http://linkedlifedata.com/resource/pubmed/id/19244519
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
2009-2-26
|
| pubmed:abstractText |
The oscillator mouse (Glra1(spd-ot)) carries a 9 bp microdeletion plus a 2 bp microinsertion in the glycine receptor alpha1 subunit gene, resulting in the absence of functional alpha1 polypeptides from the CNS and lethality 3 weeks after birth. Depending on differential use of two splice acceptor sites in exon 9 of the Glra1 gene, the mutant allele encodes either a truncated alpha1 subunit (spd(ot)-trc) or a polypeptide with a C-terminal missense sequence (spd(ot)-elg). During recombinant expression, both splice variants fail to form ion channels. In complementation studies, a tail construct, encoding the deleted C-terminal sequence, was coexpressed with both mutants. Coexpression with spd(ot)-trc produced glycine-gated ion channels. Rescue efficiency was increased by inclusion of the wild-type motif RRKRRH. In cultured spinal cord neurons from oscillator homozygotes, viral infection with recombinant C-terminal tail constructs resulted in appearance of endogenous alpha1 antigen. The functional rescue of alpha1 mutants by the C-terminal tail polypeptides argues for a modular subunit architecture of members of the Cys-loop receptor family.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
1529-2401
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
25
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| pubmed:volume |
29
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2440-52
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| pubmed:meshHeading |
pubmed-meshheading:19244519-Animals,
pubmed-meshheading:19244519-Biotinylation,
pubmed-meshheading:19244519-Cells, Cultured,
pubmed-meshheading:19244519-Cercopithecus aethiops,
pubmed-meshheading:19244519-Embryo, Mammalian,
pubmed-meshheading:19244519-Humans,
pubmed-meshheading:19244519-Ion Channel Gating,
pubmed-meshheading:19244519-Luminescent Proteins,
pubmed-meshheading:19244519-Membrane Potentials,
pubmed-meshheading:19244519-Mice,
pubmed-meshheading:19244519-Mice, Transgenic,
pubmed-meshheading:19244519-Models, Molecular,
pubmed-meshheading:19244519-Mutagenesis, Site-Directed,
pubmed-meshheading:19244519-Mutation,
pubmed-meshheading:19244519-Neurons,
pubmed-meshheading:19244519-Patch-Clamp Techniques,
pubmed-meshheading:19244519-Protein Structure, Tertiary,
pubmed-meshheading:19244519-Receptors, Glycine,
pubmed-meshheading:19244519-Spinal Cord,
pubmed-meshheading:19244519-Transfection
|
| pubmed:year |
2009
|
| pubmed:articleTitle |
Functional complementation of Glra1(spd-ot), a glycine receptor subunit mutant, by independently expressed C-terminal domains.
|
| pubmed:affiliation |
Institut für Biochemie, Emil-Fischer-Zentrum, Universität Erlangen-Nürnberg, 91054 Erlangen, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|