TOR complex 1 negatively regulates NDR kinase Cbk1 to control cell separation in budding yeast

Magdalena Foltman1,2, Iván Mendez2,3, Joan J Bech-Serra4

  • 1Mechanisms and Regulation of Cell Division Research Unit, Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Universidad de Cantabria-CSIC, Santander, Spain.

Plos Biology
|August 30, 2023
PubMed

Insights

Target of rapamycin complex 1 (TORC1) in yeast blocks cell separation after division. It achieves this by phosphorylating the Cbk1 protein kinase, impacting cell cycle progression and membrane fusion.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The target of rapamycin (TOR) pathway is crucial for coordinating cell growth and the cell cycle.
  • Mechanisms by which TOR regulates post-anaphase events, including cell separation, are not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which TOR signaling regulates cell separation in budding yeast.
  • To identify key proteins and phosphorylation events involved in TOR-mediated control of cytokinesis.

Main Methods:

  • Investigated the role of TOR complex 1 (TORC1) in budding yeast cell separation.
  • Utilized phosphomimetic substitution to analyze Cbk1 kinase activity.
  • Identified Sec3 as a substrate of Cbk1 and examined its interaction with SNARE components.

Main Results:

  • TORC1 was found to inhibit cell separation by phosphorylating the NDR kinase Cbk1.
  • Phosphorylation at residue T574 of Cbk1 was identified as critical for TORC1's control over cell separation.
  • TORC1 activity was shown to disrupt the interaction between Sec3 and t-SNARE, hindering membrane fusion.

Conclusions:

  • TORC1 negatively regulates cell separation in budding yeast through Cbk1 phosphorylation.
  • This pathway controls the fusion of secretory vesicles at the division site, impacting cytokinesis completion.

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