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Gene Review

SCP160  -  Scp160p

Saccharomyces cerevisiae S288c

Synonyms: HX, J1017, Protein HX, Protein SCP160, YJL080C
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Disease relevance of SCP160


High impact information on SCP160

  • We also show that signaling by activated Gpa1 requires direct coupling to an RNA binding protein Scp160 [2].
  • DDP1 is a multi-KH domain protein homologous to the yeast Scp160 protein that is involved in the control of cell ploidy [3].
  • The contribution of Scp160p to silencing is independent of its binding to the ribosome as deletion of the last two KH domains, which mediate ribosomal binding, has no effect on silencing [4].
  • Disruption of SCP160 increases cell ploidy but this effect is also independent of the contribution of Scp160p to telomeric silencing as strong relief of silencing is observed in Deltascp160 cells with normal ploidy and, vice versa, Deltascp160 cells with highly increased ploidy show no significant silencing defects [4].
  • These results are discussed in the context of a model in which Scp160p contributes to silencing by helping telomere clustering [4].

Biological context of SCP160


Anatomical context of SCP160


Associations of SCP160 with chemical compounds

  • Furthermore, we have found that Scp160p is released from polyribosomes by EDTA in the form of a large complex of> or =1300 kDa that is sensitive both to RNase and NaCl [9].
  • Using sucrose gradient fractionation studies we have demonstrated that Scp160p in cytoplasmic lysates is predominantly associated with polyribosomes [9].

Physical interactions of SCP160

  • Scp160p is an RNA-binding protein containing 14 tandemly repeated heterogenous nuclear ribonucleoprotein K-homology domains, which are implicated in RNA binding [8].

Other interactions of SCP160

  • Finally, we probed the impact of EAP1 loss on Scp160p, and vice versa, and found that loss of each gene resulted in a significant change in either the complex associations or subcellular distribution of the other protein [6].
  • These findings suggest an additional role for Gpa1 and reveal Scp160 as a component of the mating response pathway in yeast [2].
  • Finally, we report that loss of Bfr1p disrupts the interaction of Scp160p with polyribosomes, thereby demonstrating that the relationship between these two proteins is functional as well as physical [10].
  • The interaction of Scp160p with ribosomes depends on Asc1p [11].
  • Using affinity-chromatography to isolate these complexes, we have identified two protein components other than Scp160p: poly(A) binding protein, Pab1p, and Bfr1p [9].

Analytical, diagnostic and therapeutic context of SCP160


  1. Histiocytosis X of the vulva with a confusing clinical and pathologic presentation. A case report. Savell, V., Hanna, R., Benda, J.A., Argenyi, Z.B. The Journal of reproductive medicine. (1995) [Pubmed]
  2. The yeast G protein alpha subunit Gpa1 transmits a signal through an RNA binding effector protein Scp160. Guo, M., Aston, C., Burchett, S.A., Dyke, C., Fields, S., Rajarao, S.J., Uetz, P., Wang, Y., Young, K., Dohlman, H.G. Mol. Cell (2003) [Pubmed]
  3. DDP1, a single-stranded nucleic acid-binding protein of Drosophila, associates with pericentric heterochromatin and is functionally homologous to the yeast Scp160p, which is involved in the control of cell ploidy. Cortés, A., Huertas, D., Fanti, L., Pimpinelli, S., Marsellach, F.X., Piña, B., Azorín, F. EMBO J. (1999) [Pubmed]
  4. The multi-KH domain protein of Saccharomyces cerevisiae Scp160p contributes to the regulation of telomeric silencing. Marsellach, F.X., Huertas, D., Azorín, F. J. Biol. Chem. (2006) [Pubmed]
  5. Scp160p, a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum, is necessary for maintenance of exact ploidy. Wintersberger, U., Kühne, C., Karwan, A. Yeast (1995) [Pubmed]
  6. Genetic and biochemical interactions between SCP160 and EAP1 in yeast. Mendelsohn, B.A., Li, A.M., Vargas, C.A., Riehman, K., Watson, A., Fridovich-Keil, J.L. Nucleic Acids Res. (2003) [Pubmed]
  7. Purification and nucleic-acid-binding properties of a Saccharomyces cerevisiae protein involved in the control of ploidy. Weber, V., Wernitznig, A., Hager, G., Harata, M., Frank, P., Wintersberger, U. Eur. J. Biochem. (1997) [Pubmed]
  8. Scp160p, an RNA-binding, polysome-associated protein, localizes to the endoplasmic reticulum of Saccharomyces cerevisiae in a microtubule-dependent manner. Frey, S., Pool, M., Seedorf, M. J. Biol. Chem. (2001) [Pubmed]
  9. Scp160p, a multiple KH-domain protein, is a component of mRNP complexes in yeast. Lang, B.D., Fridovich-Keil, J.L. Nucleic Acids Res. (2000) [Pubmed]
  10. The brefeldin A resistance protein Bfr1p is a component of polyribosome-associated mRNP complexes in yeast. Lang, B.D., Li Am, n.u.l.l., Black-Brewster, H.D., Fridovich-Keil, J.L. Nucleic Acids Res. (2001) [Pubmed]
  11. Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes. Baum, S., Bittins, M., Frey, S., Seedorf, M. Biochem. J. (2004) [Pubmed]
  12. Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast. Li, A.M., Vargas, C.A., Brykailo, M.A., Openo, K.K., Corbett, A.H., Fridovich-Keil, J.L. Nucleic Acids Res. (2004) [Pubmed]
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