Source:http://linkedlifedata.com/resource/pubmed/id/12177195
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
16
|
| pubmed:dateCreated |
2002-8-14
|
| pubmed:abstractText |
Glial fibrillary acidic protein (GFAP), the principal intermediate filament (IF) protein of mature astrocytes in the CNS, plays specific roles in astrocyte functions. GFAP has multiple phosphorylation sites at its N-terminal head domain. To examine the role of phosphorylation at these sites, we generated a series of substitution mutant mice in which phosphorylation sites (Ser/Thr) were replaced by Ala, in different combinations. Gfap(hm3/hm3) mice carrying substitutions at all five phosphorylation sites showed extensive decrease in both filament formation and amounts of GFAP. Gfap(hm1/hm1) and Gfap(hm2/hm2) mice, which carry substitutions at three of five sites and in different combinations, showed differential phenotypes. Although Gfap(hm3/hm3) mice retained GFAP filaments in Bergmann glia in the cerebellum, the (Gfap(hm3/hm3):Vim(-/-)) mice lacked GFAP filaments. Pulse-chase experiments of cultured astrocytes indicated that the Hm3-GFAP encoded by Gfap(hm3) was unstable particularly in the absence of vimentin, another IF protein. These results revealed the role of phosphorylation in turnover of GFAP and a synergistic role of GFAP and vimentin in the dynamics of glial filaments. The data further suggest that each of the phosphorylated sites has a distinct impact on the dynamics of GFAP.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
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| pubmed:issn |
1529-2401
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
15
|
| pubmed:volume |
22
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6972-9
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12177195-Animals,
pubmed-meshheading:12177195-Astrocytes,
pubmed-meshheading:12177195-Binding Sites,
pubmed-meshheading:12177195-Brain,
pubmed-meshheading:12177195-Cell Count,
pubmed-meshheading:12177195-Cells, Cultured,
pubmed-meshheading:12177195-Gene Targeting,
pubmed-meshheading:12177195-Glial Fibrillary Acidic Protein,
pubmed-meshheading:12177195-Immunohistochemistry,
pubmed-meshheading:12177195-Intermediate Filaments,
pubmed-meshheading:12177195-Mice,
pubmed-meshheading:12177195-Mice, Mutant Strains,
pubmed-meshheading:12177195-Molecular Sequence Data,
pubmed-meshheading:12177195-Mutagenesis, Site-Directed,
pubmed-meshheading:12177195-Optic Nerve,
pubmed-meshheading:12177195-Phenotype,
pubmed-meshheading:12177195-Phosphorylation,
pubmed-meshheading:12177195-Sequence Homology, Amino Acid,
pubmed-meshheading:12177195-Structure-Activity Relationship,
pubmed-meshheading:12177195-Vimentin
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Protective role of phosphorylation in turnover of glial fibrillary acidic protein in mice.
|
| pubmed:affiliation |
Laboratory for Behavioral Genetics, RIKEN Brain Science Institute, Wako 351-0198, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|