FB2026_01 , released March 12, 2026
FB2026_01 , released March 12, 2026
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Citation
Jansen, R.P., Niessing, D. (2012). Assembly of mRNA-Protein Complexes for Directional mRNA Transport in Eukaryotes - An Overview.  Curr. Protein Pept. Sci. 13(4): 284--293.
FlyBase ID
FBrf0219047
Publication Type
Review
Abstract
At all steps from transcription to translation, RNA-binding proteins play important roles in determining mRNA function. Initially it was believed that for the vast majority of transcripts the role of RNA-binding proteins is limited to general functions such as splicing and translation. However, work from recent years showed that members of this class of proteins also recognize several mRNAs via cis-acting elements for their incorporation into large motor-containing particles. These particles are transported to distant subcellular sites, where they become subsequently translated. This process, called mRNA localization, occurs along microtubules or actin filaments, and involves kinesins, dyneins, as well as myosins. Although mRNA localization has been detected in a large number of organisms from fungi to humans, the underlying molecular machineries are not well understood. In this review we will outline general principles of mRNA localization and highlight three examples, for which a comparably large body of information is available. The first example is She2p/She3p-dependent localization of ASH1 mRNA in budding yeast. It is particularly well suited to highlight the interdependence between different steps of mRNA localization. The second example is Staufen-dependent localization of oskar mRNA in the Drosophila embryo, for which the importance of nuclear events for cytoplasmic localization and translational control has been clearly demonstrated. The third example summarizes Egalitarian/Bicaudal D-dependent mRNA transport events in the oocyte and embryo of Drosophila. We will highlight general themes and differences, point to similarities in other model systems, and raise open questions that might be answered in the coming years.
PubMed ID
PubMed Central ID
PMC3474952 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Curr. Protein Pept. Sci.
    Title
    Current protein & peptide science
    ISBN/ISSN
    1389-2037 1875-5550
    Data From Reference
    Genes (18)
    Natural transposons (1)