ArticleNucleic acids research2000
Scp160p, a multiple KH-domain protein, is a component of mRNP complexes in yeast.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 54 citations in OpenAlex.
- Scp160 deletion suppresses TDP-43 aggregation and toxicity inMicrobial cell (Graz, Austria) · 2026Article
- Local translation of yeastRNA (New York, N.Y.) · 2019Article
- Tma108, a putative M1 aminopeptidase, is a specific nascent chain-associated protein in Saccharomyces cerevisiae.Nucleic acids research · 2016Article
- The RNA-binding protein vigilin regulates VLDL secretion through modulation of Apob mRNA translation.Nature communications · 2016Article
- Dissecting the expression relationships between RNA-binding proteins and their cognate targets in eukaryotic post-transcriptional regulatory networks.Scientific reports · 2016Article
- RACK1 Function in Cell Motility and Protein Synthesis.Genes & cancer · 2013Review
- Scp160-dependent mRNA trafficking mediates pheromone gradient sensing and chemotropism in yeast.Cell reports · 2012Article
- Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180.Nucleic acids research · 2012Article
- Posttranscriptional suppression of proto-oncogene c-fms expression by vigilin in breast cancer.Molecular and cellular biology · 2011Article
- Vgl1, a multi-KH domain protein, is a novel component of the fission yeast stress granules required for cell survival under thermal stress.Nucleic acids research · 2010Article
- Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiae.Biochimica et biophysica acta · 2007Review
- Functional overlap between conserved and diverged KH domains in Saccharomyces cerevisiae SCP160.Nucleic acids research · 2007Article
- Genome-scale analysis reveals Sst2 as the principal regulator of mating pheromone signaling in the yeast Saccharomyces cerevisiae.Eukaryotic cell · 2006Article
- Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae.Molecular biology of the cell · 2004Article
- Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes.The Biochemical journal · 2004Article
- Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast.Nucleic acids research · 2004Article
- Genetic and biochemical interactions between SCP160 and EAP1 in yeast.Nucleic acids research · 2003Article
- RNAi-mediated depletion of the 15 KH domain protein, vigilin, induces death of dividing and non-dividing human cells but does not initially inhibit protein synthesis.Nucleic acids research · 2003Article
- Scp160p associates with specific mRNAs in yeast.Nucleic acids research · 2003Article
- The Khd1 protein, which has three KH RNA-binding motifs, is required for proper localization of ASH1 mRNA in yeast.The EMBO journal · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Scp160p is a 160 kDa protein in the yeast Saccharomyces cerevisiae that contains 14 repeats of the hnRNP K-homology (KH) domain, and demonstrates significant sequence homology to a family of proteins collectively known as vigilins. As a first step towards defining the function of Scp160p, we have characterized the subcellular distribution and in vivo interactions of this protein. Using sucrose gradient fractionation studies we have demonstrated that Scp160p in cytoplasmic lysates is predominantly associated with polyribosomes. 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. Using affinity-chromatography to isolate these complexes, we have identified two protein components other than Scp160p: poly(A) binding protein, Pab1p, and Bfr1p. The presence of Pab1p confirms these complexes to be mRNPs. The presence of Bfr1p is intriguing because the null phenotype for this gene is essentially the same as that reported for scp160 -null cells: increased cell size and aberrant DNA content. These results demonstrate that Scp160p associates with polyribosome-bound mRNP complexes in vivo, implicating a role for this protein in one or more levels of mRNA metabolism in yeast.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.