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Human UBL5 protein interacts with coilin and meets the Cajal bodies

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F13%3A43895349" target="_blank" >RIV/60461373:22330/13:43895349 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.sciencedirect.com/science/article/pii/S0006291X13008905" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0006291X13008905</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbrc.2013.05.083" target="_blank" >10.1016/j.bbrc.2013.05.083</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Human UBL5 protein interacts with coilin and meets the Cajal bodies

  • Original language description

    UBL5 protein, a structural homologue of ubiquitin, was shown to be involved in pre-mRNA splicing and transcription regulation in yeast and Caenorhabditis elegans, respectively. However, role of the UBL5 human orthologue is still elusive. In our study, weobserved that endogenous human UBL5 that was localized in the nucleus, partially associates with Cajal bodies (CBs), nuclear domains where spliceosomal components are assembled. Simultaneous expression of exogenous UBL5 and coilin resulted in their nuclear colocalization in HeLa cells. The ability of UBL5 to interact with coilin was proved by GST pull-down assay using coilin that was either in vitro translated or extracted from HEK293T cells. Further, our results showed that the UBL5-coilin interactionwas not influenced by coilin phosphorylation. These results suggest that UBL5 could be targeted to CBs via its interaction with coilin. Relation between human UBL5 protein and CBs is in the agreement with current observations about yeast

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biochemical and Biophysical Research Communications

  • ISSN

    0006-291X

  • e-ISSN

  • Volume of the periodical

    436

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    6

  • Pages from-to

    240-245

  • UT code for WoS article

    000321601300023

  • EID of the result in the Scopus database