Transportin-SR, a Nuclear Import Receptor for SR Proteins

doi:10.1083/jcb.145.6.1145

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J. Cell Biol., Volume 145, Number 6, June 14, 1999 1145-1152

Transportin-SR, a Nuclear Import Receptor for SR Proteins

Naoyuki Kataoka, Jennifer L. Bachorik, and Gideon Dreyfuss

Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Department of Biochemistry and Biophysics, Philadelphia, Pennsylvania 19104-6148

The SR proteins, a group of abundant arginine/serine (RS)-rich proteins, are essential pre-mRNA splicing factors that arelocalized in the nucleus. The RS domain of these proteins servesas a nuclear localization signal. We found that RS domain-bearingproteins do not utilize any of the known nuclear import receptorsand identified a novel nuclear import receptor specific for SRproteins. The SR protein import receptor, termed transportin-SR(TRN-SR), binds specifically and directly to the RS domains ofASF/SF2 and SC35 as well as several other SR proteins. The nucleartransport regulator RanGTP abolishes this interaction. RecombinantTRN-SR mediates nuclear import of RS domain- bearing proteinsin vitro. TRN-SR has amino acid sequence similarity to severalmembers of the importin $beta$ /transportin family. These findings stronglysuggest that TRN-SR is a nuclear import receptor for the SR proteinfamily.

Key words: SR proteins; RS domain; nuclear localization signal; nuclear import receptor; RanGTP

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