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rdf:type |
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lifeskim:mentions |
umls-concept:C0013138,
umls-concept:C0029047,
umls-concept:C0035696,
umls-concept:C0040711,
umls-concept:C0220647,
umls-concept:C0332281,
umls-concept:C0439064,
umls-concept:C0560175,
umls-concept:C1135629,
umls-concept:C1336789,
umls-concept:C1552944,
umls-concept:C1706209
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pubmed:issue |
1-2
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pubmed:dateCreated |
2008-12-8
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pubmed:abstractText |
In Drosophila melanogaster, Cup acts as a translational regulator during oocyte maturation and early embryogenesis. In this report, we show that Cup associates with Miranda, an adaptor protein involved in localization of specific mRNA complexes in both neuroblasts and oocytes. miranda and cup also interact genetically, since reducing miranda activity worsens the oogenesis defects associated with different cup mutant alleles. miranda mRNA is first detected within the cytoplasm of egg chambers during early oogenesis, coincidentally with very low levels of Miranda protein. We furthermore show that Cup interacts with Staufen, a protein involved in mRNA localization during oogenesis and nervous system development, and the two proteins co-localize within the posterior cytoplasm of late oocytes. Our results substantiate the idea that Cup is a multi-functional protein cooperating with different protein partners to direct egg chamber development at multiple time-points.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mira protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cup protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/stau protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
428
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-52
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pubmed:meshHeading |
pubmed-meshheading:18930123-Animals,
pubmed-meshheading:18930123-Cell Cycle Proteins,
pubmed-meshheading:18930123-Crosses, Genetic,
pubmed-meshheading:18930123-Cytoplasm,
pubmed-meshheading:18930123-Drosophila Proteins,
pubmed-meshheading:18930123-Drosophila melanogaster,
pubmed-meshheading:18930123-Female,
pubmed-meshheading:18930123-Fluorescent Antibody Technique,
pubmed-meshheading:18930123-Gene Expression Regulation, Developmental,
pubmed-meshheading:18930123-Immunoprecipitation,
pubmed-meshheading:18930123-In Situ Hybridization,
pubmed-meshheading:18930123-Oocytes,
pubmed-meshheading:18930123-Oogenesis,
pubmed-meshheading:18930123-Peptide Fragments,
pubmed-meshheading:18930123-Protein Biosynthesis,
pubmed-meshheading:18930123-RNA, Messenger,
pubmed-meshheading:18930123-RNA-Binding Proteins,
pubmed-meshheading:18930123-Two-Hybrid System Techniques
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pubmed:year |
2009
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pubmed:articleTitle |
The translational repressor Cup associates with the adaptor protein Miranda and the mRNA carrier Staufen at multiple time-points during Drosophila oogenesis.
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pubmed:affiliation |
CEINGE-Biotecnologie Avanzate, Via Comunale Margherita 482, Naples, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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