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Coupled Caspase and N-End Rule Ligase Activities Allow Recognition and Degradation of Pluripotency Factor LIN-28

Benjamin P Weaver1, Yi M Weaver1, Shohei Mitani2

  • 1The Howard Hughes Medical Institute and Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.

Developmental Cell
|June 13, 2017
PubMed

Insights

The CED-3 caspase and UBR-1 E3 ligase inactivate the LIN-28 pluripotency factor in Caenorhabditis elegans stem cells. This non-apoptotic function ensures proper cell fate patterning during development.

Area of Science:

  • Cell biology
  • Developmental biology
  • Molecular genetics

Background:

  • Cell death machinery components, like caspases, have non-apoptotic roles in various organisms.
  • Mechanisms of non-canonical caspase substrate recognition and regulation of gene expression by caspases are not fully understood.

Purpose of the Study:

  • To elucidate the mechanisms of non-apoptotic caspase function in regulating gene expression and developmental patterning.
  • To investigate the interaction between caspases and the Arg/N-end rule pathway in controlling pluripotency factors.

Main Methods:

  • Utilized Caenorhabditis elegans as a model organism.
  • Investigated the roles of CED-3 caspase and UBR-1 E3 ligase in seam cells.
  • Analyzed the inactivation of the LIN-28 pluripotency factor.

Main Results:

  • CED-3 caspase and the UBR-1 E3 ligase cooperate to inactivate the LIN-28 pluripotency factor in seam cells.
  • This inactivation is crucial for proper temporal cell fate patterning.
  • CED-3 and UBR-1 function in a non-additive manner, forming a complex to degrade LIN-28.

Conclusions:

  • Caspases and E3 ligases can form complexes to mediate non-apoptotic protein inactivation.
  • This mechanism facilitates developmental program switches by regulating pluripotency factors.
  • Highlights a novel role for caspases in gene expression regulation beyond cell death.
Keywords:
Arg/N-end ruleLin28UBRdevelopmental timingheterochronicnon-apoptoticproteasomeproteostasisstem cell

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