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Related Experiment Videos

TOR signaling regulates microtubule structure and function.

J H Choi1, N R Adames, T F Chan

  • 1Departments of Pathology, Washington University School of Medicine, St Louis, MO 63110, USA.

Current Biology : CB
|July 19, 2000
PubMed
Summary
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The target of rapamycin (TOR) protein interacts with Bik1p, a microtubule-associated protein. Inhibiting TOR with rapamycin disrupts microtubule stability and cell division processes in yeast.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Microtubule-associated proteins (MAPs) dictate microtubule functional diversity and structural heterogeneity.
  • Bik1p is a MAP crucial for microtubule assembly, stability, and function in yeast cell processes like karyogamy and nuclear migration.
  • The target of rapamycin (TOR) protein is inhibited by rapamycin, a complex of the antibiotic and FKBP12.

Purpose of the Study:

  • To investigate the physical interaction between TOR and Bik1p.
  • To determine the effect of TOR inhibition on microtubule dynamics and cellular functions.
  • To elucidate the role of TOR signaling in microtubule stability and function.

Main Methods:

  • Investigated the physical interaction between TOR and Bik1p using co-immunoprecipitation or similar assays.

Related Experiment Videos

  • Utilized rapamycin to inhibit TOR activity in Saccharomyces cerevisiae.
  • Assessed microtubule assembly, elongation, and stability following TOR inhibition.
  • Examined cellular processes including spindle orientation, nuclear movement, karyogamy, and chromosomal stability.

    • Main Results:

    • TOR was found to physically interact with Bik1p, the yeast homolog of human CLIP-170/Restin.
    • Rapamycin-induced inhibition of TOR significantly impaired microtubule assembly, elongation, and stability, independent of protein synthesis.
    • TOR inhibition led to defects in spindle orientation, nuclear positioning, karyogamy, and chromosomal stability, mirroring those observed in bik1 deletion mutants.

    Conclusions:

    • TOR signaling plays a significant role in regulating microtubule stability and function.
    • Bik1p is a potential mediator of TOR's effects on microtubules.
    • The findings reveal a novel regulatory pathway involving TOR in cytoskeletal dynamics and cell division.