A role for ubiquitin in the spliceosome assembly pathway View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2008-05

AUTHORS

Priya Bellare, Eliza C Small, Xinhua Huang, James A Wohlschlegel, Jonathan P Staley, Erik J Sontheimer

ABSTRACT

The spliceosome uses numerous strategies to regulate its function in mRNA maturation. Ubiquitin regulates many cellular processes, but its potential roles during splicing are unknown. We have developed a new strategy that reveals a direct role for ubiquitin in the dynamics of splicing complexes. A ubiquitin mutant (I44A) that can enter the conjugation pathway but is compromised in downstream functions diminishes splicing activity by reducing the levels of the U4/U6-U5 small nuclear ribonucleoprotein (snRNP). Similarly, an inhibitor of ubiquitin's protein-protein interactions, ubistatin A, reduces U4/U6-U5 triple snRNP levels in vitro. When ubiquitin interactions are blocked, ATP-dependent disassembly of purified U4/U6-U5 particles is accelerated, indicating a direct role for ubiquitin in repressing U4/U6 unwinding. Finally, we show that the conserved splicing factor Prp8 is ubiquitinated within purified triple snRNPs. These results reveal a previously unknown ubiquitin-dependent mechanism for controlling the pre-mRNA splicing pathway. More... »

PAGES

444-451

References to SciGraph publications

  • 2005-08. Ubiquitin-binding domains in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • 2003-10. Global analysis of protein expression in yeast in NATURE
  • 2005-08. Ubiquitin and ubiquitin-like proteins as multifunctional signals in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • 2003-04. Structural insights into the U-box, a domain associated with multi-ubiquitination in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2003-08. A proteomics approach to understanding protein ubiquitination in NATURE BIOTECHNOLOGY
  • Journal

    TITLE

    Nature Structural & Molecular Biology

    ISSUE

    5

    VOLUME

    15

    Author Affiliations

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsmb.1401

    DOI

    http://dx.doi.org/10.1038/nsmb.1401

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1041600231

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/18425143


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    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/nsmb.1401'

    RDF/XML is a standard XML format for linked data.

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