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The F-Actin-Binding MPRIP Forms Phase-Separated Condensates and Associates with PI(4,5)P2 and Active RNA Polymerase II in the Cell Nucleus
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SYSNO ASEP 0554294 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The F-Actin-Binding MPRIP Forms Phase-Separated Condensates and Associates with PI(4,5)P2 and Active RNA Polymerase II in the Cell Nucleus Author(s) Balaban, Can (UMG-J)
Sztacho, Martin (UMG-J) ORCID
Blažíková, Michaela (UMG-J)
Hozák, Pavel (UMG-J) RID, ORCIDNumber of authors 4 Article number 848 Source Title Cells. - : MDPI
Roč. 10, č. 4 (2021)Number of pages 17 s. Publication form Online - E Language eng - English Country CH - Switzerland Keywords mprip ; phase separation ; pip2 ; actin ; nucleus Subject RIV EB - Genetics ; Molecular Biology OECD category Cell biology R&D Projects GA19-05608S GA ČR - Czech Science Foundation (CSF) GA18-19714S GA ČR - Czech Science Foundation (CSF) EF16_013/0001775 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LTC19048 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LTC20024 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2018129 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Research Infrastructure Czech-BioImaging - 90062 - Ústav molekulární genetiky AV ČR, v. v. i.
Czech-BioImaging II - 90129 - Ústav molekulární genetiky AV ČR, v. v. i.Method of publishing Open access Institutional support UMG-J - RVO:68378050 UT WOS 000642893600001 DOI 10.3390/cells10040848 Annotation Here, we provide evidence for the presence of Myosin phosphatase rho-interacting protein (MPRIP), an F-actin-binding protein, in the cell nucleus. The MPRIP protein binds to Phosphatidylinositol 4,5-bisphosphate (PIP2) and localizes to the nuclear speckles and nuclear lipid islets which are known to be involved in transcription. We identified MPRIP as a component of RNA Polymerase II/Nuclear Myosin 1 complex and showed that MPRIP forms phase-separated condensates which are able to bind nuclear F-actin fibers. Notably, the fibrous MPRIP preserves its liquid-like properties and reforms the spherical shaped condensates when F-actin is disassembled. Moreover, we show that the phase separation of MPRIP is driven by its long intrinsically disordered region at the C-terminus. We propose that the PIP2/MPRIP association might contribute to the regulation of RNAPII transcription via phase separation and nuclear actin polymerization. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2022 Electronic address https://www.mdpi.com/2073-4409/10/4/848
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