motility screen identifies drosophila igf-ii mrna-binding protein—zipcode-binding protein acting in oogenesis and synaptogenesis运动性屏幕识别果蝇igf-ii mrna-binding protein-zipcode-binding蛋白质在卵子发生和突触发生.pdfVIP

motility screen identifies drosophila igf-ii mrna-binding protein—zipcode-binding protein acting in oogenesis and synaptogenesis运动性屏幕识别果蝇igf-ii mrna-binding protein-zipcode-binding蛋白质在卵子发生和突触发生.pdf

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motility screen identifies drosophila igf-ii mrna-binding protein—zipcode-binding protein acting in oogenesis and synaptogenesis运动性屏幕识别果蝇igf-ii mrna-binding protein-zipcode-binding蛋白质在卵子发生和突触发生

Motility Screen Identifies Drosophila IGF-II mRNA-Binding Protein—Zipcode-Binding Protein Acting in Oogenesis and Synaptogenesis 1[ 1[ 1 ´ 2 3 4 Kristin L. M. Boylan , Sarah Mische , Mingang Li , Guillermo Marques , Xavier Morin , William Chia , 1* Thomas S. Hays 1 Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, United States of America, 2 Department of Cell Biology, The ´ University of Alabama at Birmingham, Birmingham, Alabama, United States of America, 3 Institut de Biologie du Developpement de Marseille-Luminy (IBDML), CNRS ´ ´ ´ UMR6216 INSERM-Universite de la Mediterrannee, Marseilles, France, 4 Temasek Life Sciences Laboratory, National University of Singapore, Singapore The localization of specific mRNAs can establish local protein gradients that generate and control the development of cellular asymmetries. While all evidence underscores the importance of the cytoskeleton in the transport and localization of RNAs, we have limited knowledge of how these events are regulated. Using a visual screen for motile proteins in a collection of GFP protein trap lines, we identified the Drosophila IGF-II mRNA-binding protein (Imp), an ortholog of Xenopus Vg1 RNA binding protein and chicken zipcode-binding protein. In Drosophila, Imp is part of a large, RNase-sensitive complex that is enriched in two polarized cell types, the developing oocyte and the neuron. Using time-lapse confocal microscopy, we establish that both dynein and kinesin contribute to the transport of GFP- Imp part

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