Lamin A/C and PI(4,5)P2-A Novel Complex in the Cell Nucleus

0584842 - ÚMG 2025 RIV CH eng J - Článek v odborném periodiku
Escudeiro Lopes, Sara Eliana - Filimonenko, Vlada - Jarolímová, Lenka - Hozák, Pavel
Lamin A/C and PI(4,5)P2-A Novel Complex in the Cell Nucleus.
Cells. Roč. 13, č. 5 (2024), č. článku 399. E-ISSN 2073-4409
Grant CEP: GA ČR GA19-05608S; GA ČR(CZ) GA18-19714S; GA ČR(CZ) GA17-09103S; GA ČR(CZ) GA16-03346S; GA ČR GA15-08738S; GA MŠMT LTC19048; GA MŠMT LTC20024; GA MŠMT(CZ) LM2018129; GA MŠMT(CZ) LM2023050; GA MŠMT(CZ) EF16_013/0001775
GRANT EU: European Commission(XE) CA15214 - EuroCellNet; European Commission(XE) CA19105 - EpiLipidNET
Institucionální podpora: RVO:68378050
Klíčová slova: phosphatidylinositol 4,5-bisphosphate * myosin-i * protein-kinase * actin * phosphorylation * transcription * progeria * binding * organization * involvement * lamin A/C * phosphorylation * cell nucleus * nuclear lamina * nucleoplasm * phosphoinositides * pi(4,5)p2 * nuclear myosin 1 * nm1
Obor OECD: Cell biology
Impakt faktor: 6, rok: 2022
Způsob publikování: Open access
https://www.mdpi.com/2073-4409/13/5/399

Lamins, the nuclear intermediate filaments, are important regulators of nuclear structural integrity as well as nuclear functional processes such as DNA transcription, replication and repair, and epigenetic regulations. A portion of phosphorylated lamin A/C localizes to the nuclear interior in interphase, forming a lamin A/C pool with specific properties and distinct functions. Nucleoplasmic lamin A/C molecular functions are mainly dependent on its binding partners, therefore, revealing new interactions could give us new clues on the lamin A/C mechanism of action. In the present study, we show that lamin A/C interacts with nuclear phosphoinositides (PIPs), and with nuclear myosin I (NM1). Both NM1 and nuclear PIPs have been previously reported as important regulators of gene expression and DNA damage/repair. Furthermore, phosphorylated lamin A/C forms a complex with NM1 in a phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2)-dependent manner in the nuclear interior. Taken together, our study reveals a previously unidentified interaction between phosphorylated lamin A/C, NM1, and PI(4,5)P2 and suggests new possible ways of nucleoplasmic lamin A/C regulation, function, and importance for the formation of functional nuclear microdomains.
Trvalý link: https://hdl.handle.net/11104/0352868