The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly

@article{Niepel2005TheNP,
  title={The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly},
  author={Mario Niepel and Caterina Strambio-de-Castillia and Joseph Fasolo and Brian T Chait and Michael P. Rout},
  journal={The Journal of Cell Biology},
  year={2005},
  volume={170},
  pages={225 - 235}
}
The two yeast proteins Mlp1p and Mlp2p (homologues of the vertebrate protein Tpr) are filamentous proteins attached to the nuclear face of nuclear pore complexes. Here we perform a proteomic analysis, which reveals that the two Mlps have strikingly different interacting partners, testifying to their different roles within the cell. We find that Mlp2p binds directly to Spc110p, Spc42p, and Spc29p, which are three core components of the spindle pole body (SPB), the nuclear envelope-associated… CONTINUE READING

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Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p.

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