Nuclear Envelope Assembly and Disassembly During the Cell Cycle

Rey‐Huei Chen, Institute of Molecular Biology, Taipei, Taiwan

Published online: September 2012

DOI: 10.1002/9780470015902.a0022532

The nuclear envelope of metazoa breaks down at the onset of mitosis and reassembles at the end of mitosis. This process is mainly controlled by the cyclin-dependent kinase that phosphorylates inner nuclear membrane (INM) proteins to disrupt their association with chromatin and to disintegrate the nuclear lamina. Upon nuclear envelope breakdown, the nuclear membrane and integral nuclear membrane proteins retract into the endoplasmic reticulum (ER), whereas other peripheral nuclear membrane proteins and some components of the nuclear pore complex become disperse in the cytosol. At late anaphase, inactivation of the cyclin-dependent kinase and dephosphorylation of INM proteins allow these proteins to bind the chromatin and brings the ER membrane to the chromatin surface to initiate nuclear envelope assembly around the compact chromosome mass. The nuclear envelope disassembly and assembly are thus coordinated with the segregation of sister chromatids in each cell division cycle to maintain genome stability.

Key Concepts:

  • The nuclear envelope is a dynamic structure that is continuous with the ER.
  • The INM proteins associate with and organise the chromatin.
  • The disassembly of nuclear envelope is triggered by the cyclin-dependent kinase at the onset of mitosis.
  • Phosphorylation of INM proteins disrupts their interaction with chromatin.
  • Nuclear envelope breakdown is essential for sister chromatid segregation.
  • Integral nuclear membrane proteins diffuse into the ER after nuclear envelope breakdown.
  • The nuclear envelope reassembles around compact chromosome mass at late anaphase/telophase.
  • Nuclear envelope reassembly is mediated by multiple interactions of the INM proteins with chromatin.
  • Dephosphorylation of INM proteins at late anaphase/telophase is required for nuclear envelope reassembly.

Keywords: nuclear envelope; endoplasmic reticulum; mitosis; inner nuclear membrane protein; phosphorylation

Figure 1. General structure of the NE and its major components. The NE is composed of a double membrane that is joined at the nuclear pore complex (NPC) insertion site and bridged by the SUN–KASH complex. The ONM is continuous with the ER dubbed with ribosomes, and the INM is enriched for integral membrane proteins such as LBR, LAP1/2, emerin, and MAN1. The latter three contain LEM domain that binds BAF. Underlying the INM is the nuclear lamina made of lamin proteins. The nuclear lamina and INM proteins mediate chromatin association with the NE.
Figure 2. Process of NE disassembly. NEBD begins with tearing and stretching of the NE by microtubules and the motor protein dynein. Upon phosphorylation by mitotic kinases, the nuclear lamina disassembles and the INM proteins detach from the chromatin. The nuclear membrane and its integral membrane proteins then disperse throughout the ER, whereas the peripheral nuclear membrane proteins become cytosolic.
Figure 3. Two distinct mechanisms of NE assembly. LBR and lamin B first target the ER to the rim of the anaphase chromosome mass, followed by membrane expansion toward the polar and equatorial regions. After the initial binding to the chromatin, LBR and lamin B become quickly enriched on the chromosomal side of the reforming NE. On the other hand, microtubules localise BAF to the core region of the chromosome mass near the spindle microtubules. BAF recruits LEM domain proteins to the core to form a stable higher-order structure that eliminates microtubules from the chromosome. All these proteins become evenly distributed on the complete NE.
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Related Sub-Topics:

Cell Membranes | Cell Cytoskeleton | Cell Compartments and Cellular Organelles | Cell Cycle
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Article Title: Nuclear Envelope Assembly and Disassembly During the Cell Cycle
 
How to Cite close
Chen, Rey‐Huei(Sep 2012) Nuclear Envelope Assembly and Disassembly During the Cell Cycle. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0022532]