Dynein light chain-dependent dimerization of Egalitarian is essential for maintaining oocyte fate in Drosophila
Autor: | Hannah Neiswender, Graydon B. Gonsalvez, Chandler H. Goldman, Rajalakshmi Veeranan-Karmegam |
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Rok vydání: | 2021 |
Předmět: |
Leucine zipper
animal structures Protein Conformation Dynein Mutant Biology Immunoglobulin light chain Article 03 medical and health sciences Oogenesis 0302 clinical medicine Cell polarity medicine Molecular motor Animals Drosophila Proteins RNA Messenger Molecular Biology 030304 developmental biology Leucine Zippers 0303 health sciences Messenger RNA Chemistry Ovary fungi Dyneins RNA Cell Biology Oocyte Phenotype Cell biology medicine.anatomical_structure embryonic structures Oocytes Drosophila Female Mutant Proteins Protein Multimerization 030217 neurology & neurosurgery Protein Binding Developmental Biology |
Zdroj: | Dev Biol |
ISSN: | 0012-1606 |
Popis: | Egalitarian (Egl) is an RNA adaptor for the Dynein motor and is thought to link numerous, perhaps hundreds, of mRNAs with Dynein. Dynein, in turn, is responsible for the transport and localization of these mRNAs. Studies have shown that efficient mRNA binding by Egl requires the protein to dimerize. We recently demonstrated that Dynein light chain (Dlc) is responsible for facilitating the dimerization of Egl. Mutations in Egl that fail to interact with Dlc do not dimerize, and as such, are defective for mRNA binding. Consequently, this mutant does not efficiently associate with BicaudalD (BicD), the factor responsible for linking the Egl/mRNA complex with Dynein. In this report, we tested whether artificially dimerizing this Dlc-binding mutant using a leucine zipper would restore mRNA binding and rescue mutant phenotypes in vivo. Interestingly, we found that although artificial dimerization of Egl restored BicD binding, it only partially restored mRNA binding. As a result, Egl-dependent phenotypes, such as oocyte specification and mRNA localization, were only partially rescued. We hypothesize that Dlc-mediated dimerization of Egl results in a three-dimensional conformation of the Egl dimer that is best suited for mRNA binding. Although the leucine zipper restores Egl dimerization, it likely does not enable Egl to assemble into the conformation required for maximal mRNA binding activity. |
Databáze: | OpenAIRE |
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