1. Nuclear Envelope Budding Enables Large Ribonucleoprotein Particle Export during Synaptic Wnt Signaling
- Author
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Alex Chun Koon, Sean D. Speese, Young-Tae Chang, John J. Nunnari, Vivian Budnik, Romina Barria, Qian Li, Yihang Li, James A. Ashley, Bulent Ataman, Vahbiz Jokhi, and Melissa J. Moore
- Subjects
Nuclear Envelope ,Muscle Fibers, Skeletal ,Cell ,Nucleoplasmic reticulum ,Neuromuscular Junction ,Biology ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,0302 clinical medicine ,Protein biosynthesis ,medicine ,Animals ,Drosophila Proteins ,Humans ,RNA, Messenger ,Nuclear export signal ,Ribonucleoprotein ,030304 developmental biology ,Envelope (waves) ,0303 health sciences ,Budding ,Biochemistry, Genetics and Molecular Biology(all) ,Ribonucleoprotein particle ,Wnt signaling pathway ,Lamin Type A ,Frizzled Receptors ,Cell biology ,Drosophila melanogaster ,medicine.anatomical_structure ,Ribonucleoproteins ,Larva ,Lamin ,030217 neurology & neurosurgery ,Signal Transduction - Abstract
SummaryLocalized protein synthesis requires assembly and transport of translationally silenced ribonucleoprotein particles (RNPs), some of which are exceptionally large. Where in the cell such large RNP granules first assemble was heretofore unknown. We previously reported that during synapse development, a fragment of the Wnt-1 receptor, DFrizzled2, enters postsynaptic nuclei where it forms prominent foci. Here we show that these foci constitute large RNP granules harboring synaptic protein transcripts. These granules exit the nucleus by budding through the inner and the outer nuclear membranes in a nuclear egress mechanism akin to that of herpes viruses. This budding involves phosphorylation of A-type lamin, a protein linked to muscular dystrophies. Thus nuclear envelope budding is an endogenous nuclear export pathway for large RNP granules.PaperFlick
- Published
- 2012