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The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope
Wolfram Antonin1, Cerstin Franz, Uta Haselmann
1European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Molecular Cell
|January 5, 2005
Summary
Pom121 is essential for nuclear envelope (NE) formation during cell division, while gp210 is not. NE formation requires pom121, but this requirement is bypassed if nuclear pore complex (NPC) assembly is blocked.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The nuclear envelope (NE) disassembles during mitosis and reassembles afterward.
- Nuclear pore complexes (NPCs) facilitate transport between the nucleus and cytoplasm during interphase.
- NPCs integrate into the reforming NE at the end of mitosis.
Purpose of the Study:
- To investigate the roles of transmembrane nucleoporins pom121 and gp210 in NE formation.
- To explore the relationship between NPC assembly and NE reformation.
Main Methods:
- In vitro nuclear envelope assembly assays.
- Depletion of specific proteins (pom121, gp210, Nup107-160 complex) using experimental techniques.
- Observation of membrane vesicle binding and fusion to chromatin.
Main Results:
- Pom121 is essential for NE formation; gp210 is dispensable.
- Depletion of pom121-containing vesicles or pom121 itself inhibits NE closure.
- Pom121 becomes dispensable for NE formation when the Nup107-160 complex is depleted, indicating a link to NPC assembly.
Conclusions:
- Pom121 plays a critical role in NE formation by mediating membrane fusion.
- NE formation is functionally linked to NPC assembly.
- A checkpoint likely monitors NPC assembly status during NE reformation.