Format

Send to

Choose Destination
Cell. 2012 May 11;149(4):832-46. doi: 10.1016/j.cell.2012.03.032.

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

Author information

1
Department of Neurobiology, University of Massachusetts Medical School, Worcester, 01605, USA.

Erratum in

  • Cell. 2012 Oct 26;151(3):687-9.

Abstract

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.

Comment in

PMID:
22579286
PMCID:
PMC3371233
DOI:
10.1016/j.cell.2012.03.032
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center