Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell Nucleus
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 inter...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-02-01
|
| Series: | Cells |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4409/13/5/399 |
| _version_ | 1797264736910311424 |
|---|---|
| author | Sara Escudeiro-Lopes Vlada V. Filimonenko Lenka Jarolimová Pavel Hozák |
| author_facet | Sara Escudeiro-Lopes Vlada V. Filimonenko Lenka Jarolimová Pavel Hozák |
| author_sort | Sara Escudeiro-Lopes |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-25T00:33:39Z |
| format | Article |
| id | doaj.art-b60eb9da1a83432792bcf938489fbc38 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-04-25T00:33:39Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-b60eb9da1a83432792bcf938489fbc382024-03-12T16:41:34ZengMDPI AGCells2073-44092024-02-0113539910.3390/cells13050399Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell NucleusSara Escudeiro-Lopes0Vlada V. Filimonenko1Lenka Jarolimová2Pavel Hozák3Department of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech RepublicDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech RepublicDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech RepublicDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech RepublicLamins, 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.https://www.mdpi.com/2073-4409/13/5/399lamin A/Cphosphorylationcell nucleusnuclear laminanucleoplasmphosphoinositides |
| spellingShingle | Sara Escudeiro-Lopes Vlada V. Filimonenko Lenka Jarolimová Pavel Hozák Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell Nucleus Cells lamin A/C phosphorylation cell nucleus nuclear lamina nucleoplasm phosphoinositides |
| title | Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell Nucleus |
| title_full | Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell Nucleus |
| title_fullStr | Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell Nucleus |
| title_full_unstemmed | Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell Nucleus |
| title_short | Lamin A/C and PI(4,5)P2—A Novel Complex in the Cell Nucleus |
| title_sort | lamin a c and pi 4 5 p2 a novel complex in the cell nucleus |
| topic | lamin A/C phosphorylation cell nucleus nuclear lamina nucleoplasm phosphoinositides |
| url | https://www.mdpi.com/2073-4409/13/5/399 |
| work_keys_str_mv | AT saraescudeirolopes laminacandpi45p2anovelcomplexinthecellnucleus AT vladavfilimonenko laminacandpi45p2anovelcomplexinthecellnucleus AT lenkajarolimova laminacandpi45p2anovelcomplexinthecellnucleus AT pavelhozak laminacandpi45p2anovelcomplexinthecellnucleus |