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PIP2-Effector Protein MPRIP Regulates RNA Polymerase II Condensation and Transcription
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SYSNO ASEP 0570972 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title PIP2-Effector Protein MPRIP Regulates RNA Polymerase II Condensation and Transcription Author(s) Balaban, Can (UMG-J)
Sztacho, Martin (UMG-J) ORCID
Antiga, Ludovica (UMG-J)
Miladinović, Ana (UMG-J)
Harata, M. (JP)
Hozák, Pavel (UMG-J) RID, ORCIDNumber of authors 6 Article number 426 Source Title Biomolecules. - : MDPI
Roč. 13, č. 3 (2023)Number of pages 19 s. Language eng - English Country CH - Switzerland Keywords pip2 ; RNA polymerase II ; transcription ; phase separation ; mprip OECD category Biochemistry and molecular biology R&D Projects GA19-05608S GA ČR - Czech Science Foundation (CSF) GA18-19714S GA ČR - Czech Science Foundation (CSF) LTC19048 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LTC20024 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2018129 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) EF16_013/0001775 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UMG-J - RVO:68378050 UT WOS 000954726000001 EID SCOPUS 85151206576 DOI 10.3390/biom13030426 Annotation The specific post-translational modifications of the C-terminal domain (CTD) of the Rpb1 subunit of RNA polymerase II (RNAPII) correlate with different stages of transcription. The phosphorylation of the Ser5 residues of this domain associates with the initiation condensates, which are formed through liquid-liquid phase separation (LLPS). The subsequent Tyr1 phosphorylation of the CTD peaks at the promoter-proximal region and is involved in the pause-release of RNAPII. By implementing super-resolution microscopy techniques, we previously reported that the nuclear Phosphatidylinositol 4,5-bisphosphate (PIP2) associates with the Ser5-phosphorylated-RNAPII complex and facilitates the RNAPII transcription. In this study, we identified Myosin Phosphatase Rho-Interacting Protein (MPRIP) as a novel regulator of the RNAPII transcription that recruits Tyr1-phosphorylated CTD (Tyr1P-CTD) to nuclear PIP2-containing structures. The depletion of MPRIP increases the number of the initiation condensates, indicating a defect in the transcription. We hypothesize that MPRIP regulates the condensation and transcription through affecting the association of the RNAPII complex with nuclear PIP2-rich structures. The identification of Tyr1P-CTD as an interactor of PIP2 and MPRIP further points to a regulatory role in RNAPII pause-release, where the susceptibility of the transcriptional complex to leave the initiation condensate depends on its association with nuclear PIP2-rich structures. Moreover, the N-terminal domain of MPRIP, which is responsible for the interaction with the Tyr1P-CTD, contains an F-actin binding region that offers an explanation of how nuclear F-actin formations can affect the RNAPII transcription and condensation. Overall, our findings shed light on the role of PIP2 in RNAPII transcription through identifying the F-actin binding protein MPRIP as a transcription regulator and a determinant of the condensation of RNAPII. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2024 Electronic address https://www.mdpi.com/2218-273X/13/3/426
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