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Molecular insight into the mechanism of nuclear PIP2 regulation of RNA Polymerase II transcription

SYSNO ASEP	0555848
Document Type	O - Others
R&D Document Type	Others
Title	Molecular insight into the mechanism of nuclear PIP2 regulation of RNA Polymerase II transcription
Author(s)	Sztacho, Martin (UMG-J)_ORCID Balaban, Can (UMG-J) Šalovská, Barbora (UMG-J) Červenka, J. (CZ) Hozák, Pavel (UMG-J)_{RID, ORCID}
Year of issue	2021
Language	eng - English
Country	AT - Austria
Keywords	Phosphoinositides ; transcription ; RNA polymerase II ; phase separation
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)
	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)
Research Infrastructure	Czech-BioImaging II - 90129 - Ústav molekulární genetiky AV ČR, v. v. i.
Institutional support	UMG-J - RVO:68378050
Annotation	Specific nuclear sub-compartments that are regions of fundamental processes such as gene expression or DNA repair, contain phosphoinositides (PIPs). PIPs potentially represent signals for the localization of specific proteins into different nuclear functional domains. We performed limited proteolysis followed by label-free quantitative mass spectrometry and identified nuclear protein effectors of phosphatidylinositol 4,5-bisphosphate (PIP2). We identified 515 proteins with PIP2-binding capacity. Gene ontology analysis revealed that these proteins are involved in regulation of Pol II, mRNA splicing, transport and cell cycle. They localize to non-membrane bound organelles and are connected to actin nucleoskeleton. We provided the evidence for presence of MPRIP, an F‐actin‐binding protein in the cell nucleus. The MPRIP protein binds to 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 Pol2/Nuclear Myosin 1 complex and showed that MPRIP forms phase‐separated condensates which are able to bind nuclear F‐actin fibers. We propose a model where the PIP2/MPRIP association might contribute to the regulation of Pol2 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

Number of the records: 1