ASAP, a novel protein complex involved in RNA processing and apoptosis Journal Article


Authors: Schwerk, C.; Prasad, J.; Degenhardt, K.; Erdjument-Bromage, H.; White, E.; Tempst, P.; Kidd, V. J.; Manley, J. L.; Lahti, J. M.; Reinberg, D.
Article Title: ASAP, a novel protein complex involved in RNA processing and apoptosis
Abstract: Different isoforms of a protein complex termed the apoptosis- and splicing-associated protein (ASAP) were isolated from HeLa cell extract. ASAP complexes are composed of the polypeptides SAP18 and RNPS1 and different isoforms of the Acinus protein. 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. Addition of ASAP isoforms to in vitro splicing reactions inhibits RNA processing mediated by ASF/SF2, by SC35, or by RNPS1. Additionally, microinjection of ASAP complexes into mammalian cells resulted in acceleration of cell death. Importantly, after induction of apoptosis the ASAP complex disassembles. Taken together, our results suggest an important role for the ASAP complexes in linking RNA processing and apoptosis.
Keywords: human cell; protein domain; mammalia; cell death; cell compartmentalization; complex formation; apoptosis; protein assembly; protein protein interaction; intron; hela cells; transcription factors; stem cell; nuclear proteins; gene expression regulation; carrier proteins; alternative rna splicing; ribonucleoproteins; spliceosome; rna processing; protein isoforms; rna splicing; rna transcription; rna processing, post-transcriptional; macromolecular substances; apoptosis inducing factor; messenger rna synthesis; humans; human; priority journal; article
Journal Title: Molecular and Cellular Biology
Volume: 23
Issue: 8
ISSN: 0270-7306
Publisher: American Society for Microbiology  
Date Published: 2003-04-01
Start Page: 2981
End Page: 2990
Language: English
DOI: 10.1128/mcb.23.8.2981-2990.2003
PUBMED: 12665594
PROVIDER: scopus
PMCID: PMC152566
DOI/URL:
Notes: Export Date: 12 September 2014 -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst