Logo image
Back
Phosphorylation of Nup98 by Multiple Kinases Is Crucial for NPC Disassembly during Mitotic Entry
Journal article   Open access   Peer reviewed

Phosphorylation of Nup98 by Multiple Kinases Is Crucial for NPC Disassembly during Mitotic Entry

Eva Laurell, Katja Beck, Ksenia Krupina, Gandhi Theerthagiri, Bernd Bodenmiller, Peter Horvath, Ruedi Aebersold, Wolfram Antonin and Ulrike Kutay
Cell, Vol.144(4), pp.539-550
02/18/2011
DOI: 10.1016/j.cell.2011.01.012
PMID: 21335236
url
https://doi.org/10.1016/j.cell.2011.01.012View
Published (Version of record) Open Access

Abstract

Disassembly of nuclear pore complexes (NPCs) is a decisive event during mitotic entry in cells undergoing open mitosis, yet the molecular mechanisms underlying NPC disassembly are unknown. Using chemical inhibition and depletion experiments we show that NPC disassembly is a phosphorylation-driven process, dependent on CDK1 activity and supported by members of the NIMA-related kinase (Nek) family. We identify phosphorylation of the GLFG-repeat nucleoporin Nup98 as an important step in mitotic NPC disassembly. Mitotic hyperphos-phorylation of Nup98 is accomplished by multiple kinases, including CDK1 and Neks. Nuclei carrying a phosphodeficient mutant of Nup98 undergo nuclear envelope breakdown slowly, such that both the dissociation of Nup98 from NPCs and the permeabilization of the nuclear envelope are delayed. Together, our data provide evidence for a phosphorylation-dependent mechanism underlying disintegration of NPCs during prophase. Moreover, we identify mitotic phosphorylation of Nup98 as a rate-limiting step in mitotic NPC disassembly.
 Biochemistry & Molecular Biology Cell Biology Life Sciences & Biomedicine Science & Technology

Details

Metrics

1 Record Views
Logo image