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First published online 18 March 2003
doi: 10.1242/jcs.00409
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Research Article |
1 Medical Research Council Protein Phosphorylation Unit, Division of Cell
Signalling, University of Dundee, Dundee DD1 5EH, Scotland, UK
2 Division of Gene Regulation and Expression, School of Life Sciences,
University of Dundee, Dundee DD1 5EH, Scotland, UK
* Author for correspondence (e-mail: p.t.w.cohen{at}dundee.ac.uk)
Accepted 3 February 2003
Protein phosphatase 4 (PPP4) is a ubiquitous essential protein serine/threonine phosphatase found in higher eukaryotes. Coordinate variation of the levels of the catalytic subunit (PPP4c) and the regulatory subunit (R2) suggests that PPP4c and R2 form a heterodimeric core to which other regulatory subunits bind. Two proteins that specifically co-purify with Flag-epitope-tagged R2 expressed in HEK-293 cells were identified as Gemin3 and Gemin4. These two proteins have been identified previously as components of the Survival of Motor Neurons (SMN) protein complex, which is functionally defective in the hereditary disorder spinal muscular atrophy. Immuno-sedimentation of the epitope-tagged SMN protein complex from HeLa cells expressing CFP-SMN showed that the SMN protein interacts, as previously reported, with Gemin2 (SIP1), Gemin3 and Gemin4 and in addition associates with PPP4c. The SMN complex has been implicated in the assembly and maturation of small nuclear ribonucleoproteins (snRNPs). Expression of GFP-R2–PPP4c in HeLa cells enhances the temporal localisation of newly formed snRNPs, which is consistent with an association of R2-PPP4c with the SMN protein complex.
Key words: Gemin4, Gemin3, Spinal muscular atrophy, Spliceosome, Cajal bodies (coiled bodies), snRNP
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