Source:http://linkedlifedata.com/resource/pubmed/id/15653691
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
14
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| pubmed:dateCreated |
2005-4-4
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| pubmed:databankReference | |
| pubmed:abstractText |
The cDNAs for two isoforms (I and II) of the 14-3-3 proteins have been cloned and functionally characterized in Trypanosoma brucei. The amino acid sequences of isoforms I and II have 47 and 50% identity to the human tau isoform, respectively, with important conserved features including a potential amphipathic groove for the binding of phosphoserine/phosphothreonine-containing motifs and a nuclear export signal-like domain. Both isoforms are abundantly expressed at approximately equal levels (1-2 x 10(6) molecules/cell) and localized mainly in the cytoplasm. Knockdown by induction of double-stranded RNA of isoform I and/or II in both bloodstream and procyclic forms resulted first in a reduction of cell motility and then significant reduction in cell growth rates and morphological changes; the changes include aberrant numbers of organelles and abnormal shapes and sizes that mimic phenotypes produced by various cytokinesis inhibitors. Morphological and fluorescence-activated cell sorting analysis of the cell cycle suggested that isoforms I and II might play important roles in nuclear (G2-M transition) and cell (M-G1 transition) division. These findings indicate that the 14-3-3 proteins play important roles in cell motility, cytokinesis, and the cell cycle.
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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/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion 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 |
8
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| pubmed:volume |
280
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
14085-96
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15653691-14-3-3 Proteins,
pubmed-meshheading:15653691-Amino Acid Sequence,
pubmed-meshheading:15653691-Animals,
pubmed-meshheading:15653691-Cell Cycle,
pubmed-meshheading:15653691-Cell Movement,
pubmed-meshheading:15653691-Cell Shape,
pubmed-meshheading:15653691-Cytokinesis,
pubmed-meshheading:15653691-Humans,
pubmed-meshheading:15653691-Mice,
pubmed-meshheading:15653691-Molecular Sequence Data,
pubmed-meshheading:15653691-Okadaic Acid,
pubmed-meshheading:15653691-Phosphoprotein Phosphatases,
pubmed-meshheading:15653691-Protein Isoforms,
pubmed-meshheading:15653691-Protozoan Proteins,
pubmed-meshheading:15653691-RNA Interference,
pubmed-meshheading:15653691-Recombinant Fusion Proteins,
pubmed-meshheading:15653691-Sequence Alignment,
pubmed-meshheading:15653691-Trypanosoma brucei brucei
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| pubmed:year |
2005
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| pubmed:articleTitle |
The 14-3-3 proteins of Trypanosoma brucei function in motility, cytokinesis, and cell cycle.
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| pubmed:affiliation |
Department of Parasitology, Kurume University School of Medicine, 67 Asahi-machi, Kurume, Fukuoka 830-0011, Japan. inouedna@med.kurume-u.ac.jp
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| pubmed:publicationType |
Journal Article
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