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

Sean D. Speese, James Ashley, Vahbiz Jokhi, John Nunnari, Romina Barria, Yihang Li, Bulent Ataman, Alex Koon, Young Tae Chang, Qian Li, Melissa J. Moore, Vivian Budnik

Research output: Contribution to journalArticle

197 Scopus citations

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. PaperFlick:

Original languageEnglish (US)
Pages (from-to)832-846
Number of pages15
JournalCell
Volume149
Issue number4
DOIs
StatePublished - May 11 2012

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Speese, S. D., Ashley, J., Jokhi, V., Nunnari, J., Barria, R., Li, Y., Ataman, B., Koon, A., Chang, Y. T., Li, Q., Moore, M. J., & Budnik, V. (2012). Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling. Cell, 149(4), 832-846. https://doi.org/10.1016/j.cell.2012.03.032