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First published online April 23, 2007

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One-way traffic for snRNPs

The mammalian nucleus contains many structures through which proteins and ribonucleoproteins (RNPs) constantly and rapidly move. On p. 1540, Judith Sleeman uses dynamic live-cell microscopy to investigate the unidirectional movement of small nuclear (sn) RNPs through the nucleus. snRNPs (essential splicing factors that contain a uridine-rich snRNA and seven Sm proteins) are assembled in the cytoplasm and then imported into the nucleus, where they pass through Cajal bodies (CBs; spherical nuclear structures where snRNPs mature) to speckles (where mature splicing factors localise). Using fluorescently tagged Sm proteins, Sleeman shows that at steady state, snRNPs exchange freely in both directions between CBs and speckles. By contrast, newly imported snRNPs interact with CBs but not speckles and also exchange with the cytoplasm. Treatment of cells with an inhibitor of CRM1, a protein required for export of snRNA out of the nucleus, she reports, reduces the time spent by snRNPs in CBs. This result identifies CRM1 as a key regulator of the trafficking of snRNPs within as well as out of the mammalian nucleus.

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Related articles in JCS:

A regulatory role for CRM1 in the multi-directional trafficking of splicing snRNPs in the mammalian nucleus

Judith Sleeman
JCS 2007 120: 1540-1550. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?