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Pellino 1 inactivates mitotic spindle checkpoint by targeting BubR1 for ubiquitinational degradation

Jihyun Park1, Hye-Young Park2, Suhyeon Kim3

  • 1Department of Health Sciences and Technology, SAIHST, Sungkyunkwan University, Seoul 06351, Republic of Korea.

Oncotarget
|April 15, 2017
PubMed

Insights

Pellino 1, an E3 ubiquitin ligase, disrupts the cell cycle by targeting BubR1 for degradation. This leads to chromosome aneuploidy and mitotic dysfunction, contributing to cancer development.

Area of Science:

  • Cell Biology
  • Molecular Oncology
  • Biochemistry

Background:

  • Aberrant signaling pathways drive cell cycle deregulation and cancer.
  • The mitotic spindle checkpoint prevents aneuploidy but its regulation by signaling pathways is unclear.
  • Pellino 1 is an E3 ubiquitin ligase responsive to receptor-mediated signaling.

Purpose of the Study:

  • To investigate the role of Pellino 1 in mitotic spindle checkpoint regulation.
  • To elucidate the mechanisms by which Pellino 1 influences chromosome aneuploidy.
  • To determine Pellino 1's contribution to neoplastic aneuploidy.

Main Methods:

  • Assessed Pellino 1 expression in vitro and in vivo.
  • Investigated Pellino 1 interaction with BubR1.
  • Analyzed BubR1 stability and ubiquitination.
  • Evaluated mitotic cell cycle progression and chromosome segregation.

Main Results:

  • Pellino 1 expression induced significant chromosome aneuploidy.
  • Pellino 1 directly interacted with BubR1 in a cell-cycle-dependent manner.
  • Pellino 1 mediated BubR1 degradation via ubiquitination, causing mitotic dysfunction and aneuploidy.

Conclusions:

  • Pellino 1 acts as an inhibitor of mitotic cell cycle and checkpoint homeostasis.
  • Pellino 1 contributes to the initiation and progression of neoplastic aneuploidy.
  • Targeting Pellino 1 may offer therapeutic strategies for aneuploidy-driven cancers.

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