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

Mario Niepel1, Caterina Strambio-de-Castillia, Joseph Fasolo

  • 1The Rockefeller University, New York, NY 10021, USA.

The Journal of Cell Biology
|July 20, 2005
PubMed

Insights

The yeast protein Mlp2p connects the spindle pole body (SPB) to nuclear pore complexes, ensuring proper SPB assembly and function. Loss of Mlp2p disrupts SPB formation and leads to cell division failures.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Yeast Genetics

Background:

  • Mlp1p and Mlp2p are yeast proteins homologous to vertebrate Tpr proteins.
  • These filamentous proteins are localized to the nuclear face of nuclear pore complexes.
  • Distinct roles for Mlp1p and Mlp2p are suggested by their differing interaction partners.

Purpose of the Study:

  • To investigate the distinct cellular roles of yeast Mlp proteins.
  • To determine the interaction partners of Mlp2p.
  • To elucidate the function of Mlp2p in spindle pole body (SPB) organization and function.

Main Methods:

  • Proteomic analysis to identify Mlp2p interacting partners.
  • Analysis of spindle pole body (SPB) components and structure in mlp2 mutants.
  • Genetic analysis, including synthetic lethality assays.

Main Results:

  • Mlp2p directly binds to core SPB components: Spc110p, Spc42p, and Spc29p.
  • mlp2 mutants exhibit smaller SPBs and aberrant SPB component accumulation within the nucleus.
  • Depletion of Mlp2p is synthetically lethal with mutations affecting SPB assembly.
  • Cells lacking Mlp2p show stochastic failures in cell division.

Conclusions:

  • Mlp2p acts as a crucial linker between the SPB and the peripheral Mlp assembly.
  • This linkage is essential for the efficient incorporation of components into the SPB.
  • Mlp2p plays a vital role in maintaining SPB integrity and function, impacting cell division.

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