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Gene Review

RNPS1  -  RNA binding protein S1, serine-rich domain

Homo sapiens

Synonyms: LDC2, RNA-binding protein with serine-rich domain 1, SR-related protein LDC2
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Disease relevance of RNPS1

  • Recombinant human RNPS1 expressed in baculovirus functionally synergizes with SR proteins and strongly activates splicing of both constitutively and alternatively spliced pre-mRNAs [1].

High impact information on RNPS1

  • Significantly, RNPS1 triggers NMD when tethered to the 3' untranslated region of beta-globin mRNA, demonstrating its role as a subunit of the postsplicing complex directly involved in mRNA surveillance [2].
  • Upon exon ligation, association of RNPS1, UAP56, and SRm160 is destabilized [3].
  • We conclude that RNPS1 is not only a potential regulator of alternative splicing but may also play a more fundamental role as a general activator of pre-mRNA splicing [1].
  • Biochemical purification of a pre-mRNA splicing activity from HeLa cells that stimulates distal alternative 3' splice sites in a concentration-dependent manner resulted in the identification of RNPS1, a novel general activator of pre-mRNA splicing [1].
  • RNPS1 is conserved in metazoans and has an RNA-recognition motif preceded by an extensive serine-rich domain [1].

Biological context of RNPS1

  • In contrast, RNAi of CstF-50 in combination with RNPS1 or REFs did not result in an apparent phenotype [4].
  • RNPS1 appears to be a versatile factor that regulates alternative splicing of a variety of pre-mRNAs [5].
  • To search for factors that functionally interact with RNPS1, we performed a yeast two-hybrid screen with a human cDNA library [5].
  • A second EJC protein, RNPS1, also has an ATP-dependent mobility, but SRm300, a protein that binds to SRm160 and participates with it in RNA splicing, remains immobile after ATP supplementation [6].
  • Splicing and RNPS1 tethering are shown to enhance the same steps in mRNA biogenesis and function, including mRNA 3' end processing and translation [7].

Anatomical context of RNPS1

  • Overexpression of RNPS1 in HeLa cells induced exon skipping in a model beta-globin pre-mRNA and a human tra-2 beta pre-mRNA [5].
  • Three of the EJC components, Aly/REF, RNPS1, and SRm160, are found on pre-mRNA by the time the spliceosome is formed, whereas Upf3b associates with splicing intermediates during or immediately after the first catalytic step of the splicing reaction (cleavage of exon 1 and intron-lariat formation) [8].

Physical interactions of RNPS1

  • These data indicate that the PITSLRE p110 isoforms interact with RNPS1 in vivo, and that these proteins may in turn influence some aspect of transcriptional and/or splicing regulation [9].
  • Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1 [10].

Regulatory relationships of RNPS1

  • These results suggest that SRm160 stimulates cleavage independently of its association with EJC components and that the cleavage-stimulatory activity of RNPS1 may be an indirect consequence of its ability to stimulate splicing [4].

Other interactions of RNPS1

  • Whereas SRm160 stimulated cleavage to a similar extent in the presence or absence of an active intron, stimulation of 3'-end cleavage by tethered RNPS1 is dependent on an active intron [4].
  • The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo [9].
  • Coexpression of RNPS1 with p54 cooperatively stimulated exon inclusion in an ATP synthase gamma-subunit pre-mRNA [5].
  • While Acinus had previously been implicated in apoptosis and was recently identified as a component of the spliceosome, RNPS1 has been described as a general activator of RNA processing [11].

Analytical, diagnostic and therapeutic context of RNPS1


  1. Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing. Mayeda, A., Badolato, J., Kobayashi, R., Zhang, M.Q., Gardiner, E.M., Krainer, A.R. EMBO J. (1999) [Pubmed]
  2. Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Lykke-Andersen, J., Shu, M.D., Steitz, J.A. Science (2001) [Pubmed]
  3. 5' exon interactions within the human spliceosome establish a framework for exon junction complex structure and assembly. Reichert, V.L., Le Hir, H., Jurica, M.S., Moore, M.J. Genes Dev. (2002) [Pubmed]
  4. An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation. McCracken, S., Longman, D., Johnstone, I.L., Cáceres, J.F., Blencowe, B.J. J. Biol. Chem. (2003) [Pubmed]
  5. Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo. Sakashita, E., Tatsumi, S., Werner, D., Endo, H., Mayeda, A. Mol. Cell. Biol. (2004) [Pubmed]
  6. In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160. Wagner, S., Chiosea, S., Ivshina, M., Nickerson, J.A. J. Cell Biol. (2004) [Pubmed]
  7. Exon junction complexes mediate the enhancing effect of splicing on mRNA expression. Wiegand, H.L., Lu, S., Cullen, B.R. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  8. A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex. Kataoka, N., Dreyfuss, G. J. Biol. Chem. (2004) [Pubmed]
  9. The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo. Loyer, P., Trembley, J.H., Lahti, J.M., Kidd, V.J. J. Cell. Sci. (1998) [Pubmed]
  10. Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1. Li, C., Lin, R.I., Lai, M.C., Ouyang, P., Tarn, W.Y. Mol. Cell. Biol. (2003) [Pubmed]
  11. ASAP, a novel protein complex involved in RNA processing and apoptosis. Schwerk, C., Prasad, J., Degenhardt, K., Erdjument-Bromage, H., White, E., Tempst, P., Kidd, V.J., Manley, J.L., Lahti, J.M., Reinberg, D. Mol. Cell. Biol. (2003) [Pubmed]
  12. Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation. Trembley, J.H., Tatsumi, S., Sakashita, E., Loyer, P., Slaughter, C.A., Suzuki, H., Endo, H., Kidd, V.J., Mayeda, A. Mol. Cell. Biol. (2005) [Pubmed]
  13. Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation. Harada, K., Yamada, A., Yang, D., Itoh, K., Shichijo, S. Int. J. Cancer (2001) [Pubmed]
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