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The Major Capsid Protein, VP1, of the Mouse Polyomavirus Stimulates the Activity of Tubulin Acetyltransferase 1 by Microtubule Stabilization

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F20%3A00541331" target="_blank" >RIV/86652036:_____/20:00541331 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/20:10414129 RIV/00216208:11320/20:10414129

  • Result on the web

    <a href="https://www.mdpi.com/1999-4915/12/2/227" target="_blank" >https://www.mdpi.com/1999-4915/12/2/227</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/v12020227" target="_blank" >10.3390/v12020227</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The Major Capsid Protein, VP1, of the Mouse Polyomavirus Stimulates the Activity of Tubulin Acetyltransferase 1 by Microtubule Stabilization

  • Original language description

    Viruses have evolved mechanisms to manipulate microtubules (MTs) for the efficient realization of their replication programs. Studying the mechanisms of replication of mouse polyomavirus (MPyV), we observed previously that in the late phase of infection, a considerable amount of the main structural protein, VP1, remains in the cytoplasm associated with hyperacetylated microtubules. VP1-microtubule interactions resulted in blocking the cell cycle in the G2/M phase. We are interested in the mechanism leading to microtubule hyperacetylation and stabilization and the roles of tubulin acetyltransferase 1 (alpha TAT1) and deacetylase histone deacetylase 6 (HDAC6) and VP1 in this mechanism. Therefore, HDAC6 inhibition assays, alpha TAT1 knock out cell infections, in situ cell fractionation, and confocal and TIRF microscopy were used. The experiments revealed that the direct interaction of isolated microtubules and VP1 results in MT stabilization and a restriction of their dynamics. VP1 leads to an increase in polymerized tubulin in cells, thus favoring alpha TAT1 activity. The acetylation status of MTs did not affect MPyV infection. However, the stabilization of MTs by VP1 in the late phase of infection may compensate for the previously described cytoskeleton destabilization by MPyV early gene products and is important for the observed inhibition of the G2> M transition of infected cells to prolong the S phase.

  • 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

    10607 - Virology

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Viruses

  • ISSN

    1999-4915

  • e-ISSN

  • Volume of the periodical

    12

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    22

  • Pages from-to

    227

  • UT code for WoS article

    000521256600068

  • EID of the result in the Scopus database

    2-s2.0-85079782230