Glycan analysis of Lamin A/C protein at G2/M and S phases of the cell cycle
| Autor: | Uslupehlivan, Ecem Sener, Deveci, Remziye, Sahar, Umut, Izzetoglu, Savas |
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| Rok vydání: | 2022 |
| Předmět: |
Biophysics
Monosaccharide Mitosis Urchin Paracentrotus-Lividus Structural Organization Biochemistry S Phase CapLC-ESI Mammalian O-Mannosylation Tandem Mass Spectrometry MS-MS Lectins Humans Mass-Spectrometry Phosphorylation Lamin Type B Emerin Cell Cycle Linked Glycosylation Nuclear Proteins Cell Biology General Medicine Glycan Lamin Type A Lamin A TEM Sialic Acids Sea-Urchin Gold Nuclear Lamins Sugars |
| Zdroj: | Cell biochemistry and biophysics. 80(4) |
| ISSN: | 1559-0283 |
| Popis: | During mitosis, phosphorylation and dephosphorylation of lamins triggers the nuclear envelope disassembly/assembly. However, it hasn't been known whether lamin proteins undergo any modification other than phosphorylation during the cell cycle. Glycosylation of lamin proteins is one of the less studied post-translational modification. Glycosylation and phosphorylation compete for the same positions and interplay between two modifications generate a post-translational code in the cell. Based on this, we hypothesized that glycosylation of lamin A/C protein may be important in the regulation of the structural organization of the nuclear lamina during interphase and mitosis. We analysed the glycan units of lamin A/C protein in lung carcinoma cells synchronized at G2/M and S phases via CapLC-ESI-MS/MS. Besides, the outermost glycan units were determined using lectin blotting and gold-conjugated antibody and lectin staining. TEM studies also allowed us to observe the localization of glycosylated lamin A/C protein. With this study, we determined that lamin A/C protein shows O-glycosylation at G2/M and S phases of the cell cycle. In addition to O-GlcNAcylation and O-GalNAcylation, lamin A/C is found to be contain Gal, Fuc, Man, and Sia sugars at G2/M and S phases for the first time. Having found the glycan units of the lamin A/C protein suggests that glycosylation might have a role in the nuclear organization during the cell cycle. Ege University Scientific Research Projects Coordination [17-FEN-031] This work was supported by the Ege University Scientific Research Projects Coordination (grant number 17-FEN-031). |
| Databáze: | OpenAIRE |
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