| Phosphorylation of p27(BBP)/eIF6 and its association with the cytoskeleton are developmentally regulated in Xenopus oogenesis. | |
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MedLine Citation:
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PMID: 15990955 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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p27BBP/eIF6 is an evolutionarily conserved regulator of ribosomal function. It is necessary for 60S biogenesis and impedes improper joining of 40S and 60S subunits, regulated by protein kinase C or Efl1p. No data on p27BBP/eIF6 during early development of Metazoa are available. We studied the distribution, post-translational changes and association with the cytoskeleton of p27BBP/ eIF6 during Xenopus oogenesis and early development. Results indicate that p27BBP/eIF6 is present throughout oogenesis, partly associated with 60S subunits, partly free and with little cytoskeleton bound. During prophase I, p27BBP/eIF6 is detected as a single band of 27-kDa. Upon maturation induced by progesterone or protein kinase C, a serine-phosphorylated 29 kDa isoform appears and is kept throughout development to the neurula stage. Confocal microscopy showed that the distribution of p27BBP/eIF6 and its association with the cytoskeleton varies according to oogenesis stages. Briefly, in stage 6 oocytes, p27BBP/eIF6 has a limited dot-like distribution, and does not co-localize with cytokeratin, whereas upon maturation it spreads throughout the cytoplasm. After fertilization, a large fraction coalesces around cytomembranes and a cytochalasin B-sensitive co-localization with cytokeratin occurs. RNAse removes p27BBP/eIF6 from the cytokeratin fibres. Developmental data suggest a role of p27BBP/eIF6 in controlling ribosomal availability or regulating cross-talk between ribosomes and the cytoskeleton. |
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Authors:
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R Carotenuto; N De Marco; S Biffo; M Wilding; M C Vaccaro; P C Marchisio; T Capriglione; G L Russo; C Campanella |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Cellular and molecular life sciences : CMLS Volume: 62 ISSN: 1420-682X ISO Abbreviation: Cell. Mol. Life Sci. Publication Date: 2005 Jul |
Date Detail:
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Created Date: 2005-07-21 Completed Date: 2005-09-30 Revised Date: 2008-05-06 |
Medline Journal Info:
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Nlm Unique ID: 9705402 Medline TA: Cell Mol Life Sci Country: Switzerland |
Other Details:
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Languages: eng Pagination: 1641-52 Citation Subset: IM |
Affiliation:
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Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico II, Napoli, Italy. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Blotting, Western Carrier Proteins / chemistry, metabolism* Cytoskeleton / metabolism* Electrophoresis, Polyacrylamide Gel Eukaryotic Initiation Factors Female Immunohistochemistry Intermediate Filament Proteins / chemistry, metabolism* Male Meiosis Microscopy, Confocal Molecular Weight Oocytes / drug effects, growth & development, metabolism Oogenesis* Phosphoric Monoester Hydrolases / metabolism Phosphorylation Phosphoserine / metabolism Progesterone / pharmacology Protein Binding Ribosomes / metabolism Time Factors Xenopus Proteins / chemistry, metabolism* Xenopus laevis Zygote / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/EIF6 protein, human; 0/Eukaryotic Initiation Factors; 0/Intermediate Filament Proteins; 0/Xenopus Proteins; 0/eIF6 protein, Xenopus; 17885-08-4/Phosphoserine; 57-83-0/Progesterone; EC 3.1.3.-/Phosphoric Monoester Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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