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Monitoring of nucleophosmin oligomerization in live cells

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F18%3A10385095" target="_blank" >RIV/00216208:11320/18:10385095 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388955:_____/18:00490941 RIV/61388963:_____/18:00491886 RIV/00023736:_____/18:00011996

  • Result on the web

    <a href="https://doi.org/10.1088/2050-6120/aaccb9" target="_blank" >https://doi.org/10.1088/2050-6120/aaccb9</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1088/2050-6120/aaccb9" target="_blank" >10.1088/2050-6120/aaccb9</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Monitoring of nucleophosmin oligomerization in live cells

  • Original language description

    Oligomerization plays a crucial role in the function of nucleophosmin (NPM), an abundant nucleolar phosphoprotein. Two dual-color methods based on modern fluorescence confocal microscopy are applied for tracking NPM aggregates in live cells: cross-correlation Number and Brightness analysis (ccN&amp;B) combined with pulsed interleaved excitation (PIE) and fluorescence-lifetime imaging microscopy (FLIM) utilizing resonance energy transfer (FRET). HEK-293T cells were transfected with mixture of plasmids designed for tagging with fluorescent proteins so that the cells express mixed population of NPM labeled either with eGFP or mRFP1. We observe joint oligomers formed from the fluorescently labeled NPM. Having validated the in vivo methods, we study an effect of substitutions in cysteine 21 (Cys21) of the NPMN-terminus on the oligomerization to demonstrate applicability of the methods. Inhibitory effect of mutations of the Cys21 to nonpolar Ala or to aromatic Phe on the oligomerization was reported in literature using in vitro semi-native electrophoresis. However, we do not detect any break-up of the joint NPM oligomers due to the Cys21 mutations in live cells. In vivo microscopy observations are supported by an in vitro method, the GFP-Trap immunoprecipitation assay. Our results therefore show importance of utilizing several methods for detection of biologically relevant protein aggregates. In vivo monitoring of the NPM oligomerization, a potential cancer therapy target, by the presented methods offers a new way to monitor effects of drugs that are tested as NPM oligomerization inhibitors directly in live cells.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Methods and Applications in Fluorescence

  • ISSN

    2050-6120

  • e-ISSN

  • Volume of the periodical

    6

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    13

  • Pages from-to

  • UT code for WoS article

    000436971700001

  • EID of the result in the Scopus database

    2-s2.0-85051424965