Downloads and Tools

•  Article PDF
  1.82 MB PDF document

Supplementary Material

•  Supplemental Figure 3
  0 B
•  Supplemental Figure 2
  0 B
•  Supplemental Figure 1
  0 B
•  Supplemental Figure 5
  0 B
•  Supplemental Figure 4
  0 B
•  Supplemental Table 1
  67.15 KB PDF document

This is an open access article.
Print this page Email this page

Recipient's Email:

Download Citation

---

Share on Facebook

Authors: Magdalena Zaremba-Czogalla, Przemysław Gagat, Katarzyna Kozioł, Magda Dubińska-Magiera, Jacek Sikora, Michał Dadlez and Ryszard Rzepecki

Magdalena Zaremba-Czogalla

Laboratory of Nuclear Proteins, Faculty of Biotechnology, University of Wrocław, Przybyszewskiego St. 63/78, 51-148 Wrocław, Poland

Przemysław Gagat

Laboratory of Nuclear Proteins, Faculty of Biotechnology, University of Wrocław, Przybyszewskiego St. 63/78, 51-148 Wrocław, Poland

Katarzyna Kozioł

Laboratory of Nuclear Proteins, Faculty of Biotechnology, University of Wrocław, Przybyszewskiego St. 63/78, 51-148 Wrocław, Poland

Magda Dubińska-Magiera

Laboratory of Nuclear Proteins, Faculty of Biotechnology, University of Wrocław, Przybyszewskiego St. 63/78, 51-148 Wrocław, Poland

Jacek Sikora

Institute of Biochemistry and Biophysics PAS, Pawinskiego 5a 02-106 Warsaw, Poland

Michał Dadlez

Institute of Biochemistry and Biophysics PAS, Pawinskiego 5a 02-106 Warsaw, Poland; Institute of Genetics and Biotechnology, Biology Department, Warsaw University, Pawinskiego 5a, 02-106 Warsaw, Poland

Ryszard Rzepecki

Corresponding author: rzepecki@ibmb.uni.wroc.pl
Laboratory of Nuclear Proteins, Faculty of Biotechnology, University of Wrocław, Przybyszewskiego St. 63/78, 51-148 Wrocław, Poland

Preview

Abstract:

Changes in the nuclear structure and function during the cell cycle are thought to be correlated with lamins phosphorylation. Here, we report the identification of new in vivo phosphorylation sites on Drosophila melanogater lamin Dm using immunoisolation and mass spectrometry with collision-induced peptide fragmentation (Electrospray-Linear Trap Quadrupole- Fourier Transform Ion Cyclotron Resonance MS/MS). We identified S19 and confirmed previously suggested S595 as phosphorylated amino acid residues on embryonic lamin Dm. We also found that T597 is phosphorylated in vivo in cultured Kc cells while S595 in embryos, which suggests that different neighboring phosphoacceptors may be modified within the same region. We demonstrate also that Drosophila melanogaster lamin Dm in very early (syncytial) embryos is almost completely dispersed through the entire embryo. Only fraction of lamin Dm is associated with nuclei and nuclear envelopes. In later stages, due to the synchronization of mitosis, lamin Dm may be both nuclear and cytoplasmic in the same embryo. Our results provide a new and essential data for better understanding of the lamin phosporylation in development and cell cycle regulation in Drosophila.