Document Detail

Squid, Cup, and PABP55B function together to regulate gurken translation in Drosophila.
MedLine Citation:
PMID:  18082158     Owner:  NLM     Status:  MEDLINE    
During Drosophila melanogaster oogenesis, the proper localization of gurken (grk) mRNA and protein is required for the establishment of the dorsal-ventral axis of the egg and future embryo. Squid (Sqd) is an RNA-binding protein that is required for the correct localization and translational regulation of the grk message. We show that Cup and polyA-binding protein (PABP) interact physically with Sqd and with each other in ovaries. We show that cup mutants lay dorsalized eggs, enhance dorsalization of weak sqd alleles, and display defects in grk mRNA localization and Grk protein accumulation. In contrast, pAbp mutants lay ventralized eggs and enhance grk haploinsufficiency. PABP also interacts genetically and biochemically with Encore. These data predict a model in which Cup and Sqd mediate translational repression of unlocalized grk mRNA, and PABP and Enc facilitate translational activation of the message once it is fully localized to the dorsal-anterior region of the oocyte. These data also provide the first evidence of a link between the complex of commonly used trans-acting factors and Enc, a factor that is required for grk translation.
K Nicole Clouse; Scott B Ferguson; Trudi Schüpbach
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-11-19
Journal Detail:
Title:  Developmental biology     Volume:  313     ISSN:  1095-564X     ISO Abbreviation:  Dev. Biol.     Publication Date:  2008 Jan 
Date Detail:
Created Date:  2008-01-14     Completed Date:  2008-02-26     Revised Date:  2014-09-17    
Medline Journal Info:
Nlm Unique ID:  0372762     Medline TA:  Dev Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  713-24     Citation Subset:  IM    
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MeSH Terms
Body Patterning
Drosophila / genetics,  metabolism,  physiology*
Drosophila Proteins / biosynthesis,  genetics,  isolation & purification,  metabolism*
Egg Proteins / genetics,  metabolism
In Situ Hybridization
Models, Biological
Oocytes / metabolism,  physiology
Oogenesis / physiology
Ovary / cytology,  metabolism,  physiology
Poly(A)-Binding Proteins / genetics,  metabolism
Precipitin Tests
Protein Binding
Protein Biosynthesis*
RNA, Messenger / metabolism
RNA-Binding Proteins / genetics,  isolation & purification,  metabolism*
Transforming Growth Factor alpha / biosynthesis,  genetics,  metabolism*
Grant Support
P01 CA041086/CA/NCI NIH HHS; P01 CA041086-200006/CA/NCI NIH HHS; P01 CA41086/CA/NCI NIH HHS; R01 GM077620/GM/NIGMS NIH HHS; R01 GM077620/GM/NIGMS NIH HHS; R01 GM077620-01A1/GM/NIGMS NIH HHS; //Howard Hughes Medical Institute
Reg. No./Substance:
0/Drosophila Proteins; 0/Egg Proteins; 0/PABP55B protein, Drosophila; 0/Poly(A)-Binding Proteins; 0/RNA, Messenger; 0/RNA-Binding Proteins; 0/Transforming Growth Factor alpha; 0/cup protein, Drosophila; 0/encore protein, Drosophila; 0/gurken protein, Drosophila; 0/squid protein, Drosophila

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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