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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

C. Balaban, M. Sztacho, M. Blažíková, P. Hozák

. 2021 ; 10 (4) : . [pub] 20210408

Language English Country Switzerland

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc22004463

Grant support
19 05608S, 18 19714S Grantová Agentura České Republiky
JSPS 20 06 Czech Academy of Sciences
RVO: 68378050 Institute of Molecular Genetics of the Czech Academy of Sciences
CZ.02.1.01/0.0/0.0/16_013/0001775 European Regional Development Fund Project
CZ.1.05/1.1.00/02.0109 European Regional Development Fund
LTC19048, LTC20024 Ministry of Education, Youth and Sports of Czech Republic COST Inter excellence internship
CA15214 EuroCellNet COST Action
LM2018129 Ministry of Education, Youth and Sports of Czech Republic - Czech BioImaging

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.

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