GSBS Student Publications


Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling

Student Author(s)

Vahbiz Jokhi; Yihang Li; Bulent Ataman; Alex Koon

GSBS Program


UMMS Affiliation

Department of Neurobiology; Department of Biochemistry and Molecular Pharmacology; Budnik Lab; Graduate School of Biomedical Sciences, Neuroscience Program



Document Type


Medical Subject Headings

Animals; Drosophila Proteins; Drosophila melanogaster; Frizzled Receptors; Humans; Lamin Type A; Larva; Muscle Fibers, Skeletal; Neuromuscular Junction; Nuclear Envelope; RNA, Messenger; Ribonucleoproteins; Signal Transduction


Biochemistry, Biophysics, and Structural Biology | Neuroscience and Neurobiology


Localized 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.


Citation: Cell. 2012 May 11;149(4):832-46. Link to article on publisher's site

Related Resources

Link to article in PubMed

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