Compartmentalization of the cell nucleus by phosphoinositides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F21%3A00555829" target="_blank" >RIV/68378050:_____/21:00555829 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Compartmentalization of the cell nucleus by phosphoinositides

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Compartmentalization of the cell nucleus by phosphoinositides

Popis výsledku anglicky

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.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10601 - Cell biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

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