Source:http://linkedlifedata.com/resource/pubmed/id/15652353
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-1-17
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pubmed:abstractText |
TRAP1 (tumor necrosis factor receptor-associated protein 1) is a member of the molecular chaperone HSP90 (90-kDa heat shock protein) family. In this study, we mainly examined the behavior of Dictyostelium TRAP1 homologue, Dd-TRAP1, during Dictyostelium development by immunoelectron microscopy. In vegetatively growing D. discoideum Ax-2 cells, Dd-TRAP1 locates in nucleolus and vesicles in addition to the cell cortex including cell membrane. Many of Dd-TRAP1 molecules moved to the mitochondrial matrix in response to differentiation, although Dd-TRAP1 on the cell membrane seems to be retained. Some Dd-TRAP1 was also found to be secreted to locate outside the cell membrane in Ax-2 cells starved for 6 h. At the multicellular slug stage, Dd-TRAP1 was primarily located in mitochondria and cell membrane in both prestalk and prespore cells. More importantly, in differentiating prespore cells, a significant number of Dd-TRAP1 locates in the PSV (prespore-specific vacuole) that is a sole cell type-specific organelle and essential for spore wall formation, whereas some Dd-TRAP1 in the cell cortical region of prestalk cells. These findings strongly suggest the importance of Dd-TRAP1 regulated temporally and spatially during Dictyostelium development. Incidentally, we also have certified that the glucose-regulated protein 94 (Dd-GRP94) is predominantly located in Golgi vesicles and cisternae, followed by its colocalization with Dd-TRAP1 in the PSV.
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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/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/glucose-regulated proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
303
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
415-24
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15652353-Animals,
pubmed-meshheading:15652353-Dictyostelium,
pubmed-meshheading:15652353-Gene Expression Regulation, Developmental,
pubmed-meshheading:15652353-HSP70 Heat-Shock Proteins,
pubmed-meshheading:15652353-HSP90 Heat-Shock Proteins,
pubmed-meshheading:15652353-Membrane Proteins,
pubmed-meshheading:15652353-Microscopy, Immunoelectron,
pubmed-meshheading:15652353-Mitochondria,
pubmed-meshheading:15652353-Models, Biological,
pubmed-meshheading:15652353-Protozoan Proteins,
pubmed-meshheading:15652353-RNA, Messenger,
pubmed-meshheading:15652353-RNA, Protozoan,
pubmed-meshheading:15652353-Vacuoles
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pubmed:year |
2005
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pubmed:articleTitle |
Changes in spatial and temporal localization of Dictyostelium homologues of TRAP1 and GRP94 revealed by immunoelectron microscopy.
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pubmed:affiliation |
Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences, Tohoku University, Aoba, Sendai 980-8578, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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