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The SUN protein Mps3 controls Ndc1 distribution and function on the nuclear membrane
Jingjing Chen1, Christine J Smoyer, Brian D Slaughter
1Stowers Institute for Medical Research, Kansas City, MO 64110.
The Journal of Cell Biology
|February 12, 2014
Summary
Ndc1 protein interacts with Mps3 at the nuclear envelope, crucial for spindle pole body duplication in yeast. This interaction
Area of Science:
- Cell biology
- Molecular genetics
- Biochemistry
Background:
- Nuclear pore complexes (NPCs) and spindle pole bodies (SPBs) assemble within the nuclear envelope (NE) during closed mitosis.
- Ndc1 is a conserved integral membrane protein essential for the insertion of both NPCs and SPBs.
Purpose of the Study:
- To investigate the interaction between Ndc1 and Mps3 at the NE.
- To elucidate the functional significance of the Ndc1-Mps3 binding in yeast cell division.
Main Methods:
- Fluorescence cross-correlation spectroscopy (FCCS) to detect Ndc1-Mps3 interaction in live yeast cells.
- Genetic and molecular analysis of novel ndc1 alleles.
- Analysis of SPB duplication and NPC assembly.
Main Results:
- Ndc1 directly interacts with the SUN domain protein Mps3 at the NE.
- A specific ndc1 allele (ndc1-L562S) disrupts Ndc1-Mps3 binding and causes lethal SPB duplication defects.
- Deletion of POM152 suppresses the growth and Mps3 binding defects of ndc1-L562S, suggesting a role in Ndc1 distribution.
Conclusions:
- The Ndc1-Mps3 interaction is vital for proper SPB duplication.
- Ndc1's localization and function are regulated by its interaction with Mps3, influencing its distribution between NPC and SPB.
- This interaction provides a critical control point for nuclear envelope-associated complex assembly.
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