The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
The Methylosome, a 20S Complex Containing JBP1 and pICln, Produces Dimethylarginine-Modified Sm Proteins
Open accessAbstract
snRNPs, integral components of the pre-mRNA splicing machinery, consist of seven Sm proteins which assemble in the cytoplasm as a ring structure on the snRNAs U1, U2, U4, and U5. The survival motor neuron (SMN) protein, the spinal muscular atrophy disease gene product, is crucial for snRNP core particle assembly in vivo. SMN binds preferentially and directly to the symmetrical dimethylarginine (sDMA)-modified arginine- and glycine-rich (RG-rich) domains of SmD1 and SmD3. We found that the unmodified, but not the sDMA-modified, RG domains of SmD1 and SmD3 associate with a 20S methyltransferase complex, termed the methylosome, that contains the methyltransferase JBP1 and a JBP1-interacting protein, pICln. JBP1 binds SmD1 and SmD3 via their RG domains, while pICln binds the Sm domains. JBP1 produces sDMAs in the RG domain-containing Sm proteins. We further demonstrate the existence of a 6S complex that contains pICln, SmD1, and SmD3 but not JBP1. SmD3 from the methylosome, but not that from the 6S complex, can be transferred to the SMN complex in vitro. Together with previous results, these data indicate that methylation of Sm proteins by the methylosome directs Sm proteins to the SMN complex for assembly into snRNP core particles and suggest that the methylosome can regulate snRNP assembly.
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Cites
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Self-citationIdentification and characterization of a spinal muscular atrophy-determining gene
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Regulation of Transcription by a Protein Methyltransferase
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Self-citationThe SMN–SIP1 Complex Has an Essential Role in Spliceosomal snRNP Biogenesis
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Self-citationA Novel Function for SMN, the Spinal Muscular Atrophy Disease Gene Product, in Pre-mRNA Splicing
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A day in the life of the spliceosome
Matera, A. G., & Wang, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3742 · Cited by 1,074
Spinal muscular atrophy: why do low levels of survival motor neuron protein make motor neurons sick?
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MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells
Kryukov, G. V., Wilson, F. H., Ruth, J. R., Paulk, J., Tsherniak, A., Marlow, S. E., Vazquez, F., Weir, B. A., Fitzgerald, M. E., Tanaka, M., et al. (2016) · Science · doi:10.1126/science.aad5214 · Cited by 688
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Metadata
- Authors
- Friesen, W. J., Paushkin, S., Wyce, A., Massenet, S., Pesiridis, G. S., Van Duyne, G., Rappsilber, J., Mann, M., & Dreyfuss, G.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2001-12-01
- Volume
- 21
- Issue
- 24
- Pages
- 8289-8300
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2137891310
- Cited by
- 408
- References
- 53
- FWCI
- 5.75
- Type
- journal article
- Language
- en
- Open access
- green
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- Friesen, W. J., Paushkin, S., Wyce, A., Massenet, S., Pesiridis, G. S., Van Duyne, G., Rappsilber, J., Mann, M., & Dreyfuss, G. (2001). The Methylosome, a 20S Complex Containing JBP1 and pICln, Produces Dimethylarginine-Modified Sm Proteins. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.21.24.8289-8300.2001
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