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The promyelocytic leukemia protein PML has a pro-apoptotic activity mediated through its RING domain

K L Borden1, E J CampbellDwyer, M S Salvato

  • 1Department of Biochemistry, Dalhousie University, Halifax, N.S., Canada. kborden@is.dal.ca

FEBS Letters
|December 31, 1997
PubMed

Insights

Promyelocytic leukemia protein (PML) promotes apoptosis. Viral infection relocates PML, enhancing cell survival against serum starvation, suggesting PML

Area of Science:

  • Cell biology
  • Virology
  • Molecular biology

Background:

  • The promyelocytic leukemia protein (PML) forms nuclear bodies crucial for cellular processes.
  • PML dysfunction is implicated in diseases like acute promyelocytic leukemia.
  • Viral infections can alter the localization and function of cellular proteins.

Purpose of the Study:

  • To investigate the role of PML in apoptosis during viral infection.
  • To determine if PML relocation affects cellular resistance to serum starvation-induced apoptosis.
  • To identify the PML domain responsible for its pro-apoptotic activity.

Main Methods:

  • Single-stranded RNA virus infection of cells.
  • Monitoring of PML body localization (nuclear vs. cytoplasmic).
  • Assessment of apoptosis resistance under serum starvation.
  • Use of antisense PML oligonucleotides.
  • Transient transfection studies to map functional domains.

Main Results:

  • Viral infection relocated PML bodies to the cytoplasm.
  • PML-relocated cells exhibited increased resistance to serum starvation-induced apoptosis.
  • Antisense PML oligonucleotides enhanced cell survival during serum deprivation.
  • The RING finger domain of PML was identified as mediating its pro-apoptotic function.

Conclusions:

  • PML plays a pro-apoptotic role, mediated by its RING finger domain.
  • Viral relocation of PML bodies contributes to enhanced cell survival.
  • Viruses may exploit PML to dysregulate host apoptosis for persistent infection.

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