MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly.
The metazoan nuclear envelope (NE) breaks down and re-forms during each cell cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport during interphase, assemble into the re-forming NE at the end of mitosis. Using in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal effect lethal), a recently discovered NE component in Caenorhabditis elegans, functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107-160 complex (Nup for nucleoporin), an important building block of the NPC, and is essential for the recruitment of the Nup107-160 complex to chromatin. We suggest that MEL-28 acts as a seeding point for NPC assembly.
Franz
Cerstin
C
European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg 69117, Germany.
Walczak
Rudolf
R
Yavuz
Sevil
S
Santarella
Rachel
R
Gentzel
Marc
M
Askjaer
Peter
P
Galy
Vincent
V
Hetzer
Martin
M
Mattaj
Iain W
IW
Antonin
Wolfram
W
D000818:Animals; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism*; D002453:Cell Cycle / Q000502:physiology*; D002843:Chromatin / Q000378:metabolism*; D004268:DNA-Binding Proteins; D004926:Escherichia coli; D005455:Fluorescent Antibody Technique; D006801:Humans; D022022:Nuclear Pore / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D034622:RNA Interference; D034741:RNA, Small Interfering / Q000235:genetics; D014981:Xenopus
D029742:Caenorhabditis elegans Proteins; D002843:Chromatin; D004268:DNA-Binding Proteins; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; D034741:RNA, Small Interfering; C514979:mel-28 protein, C elegans