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Microtubule-associated protein 1 light chain 3 interacts with and contributes to growth inhibiting effect of PML

Wei He1, Chuan-Xi Hu1, Jia-Kai Hou2

  • 1Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine (SJTU-SM), Shanghai, China.

Plos One
|November 25, 2014
PubMed

Insights

Promyelocytic leukemia (PML) protein interacts with microtubule-associated protein light chain 3 (LC3) in the nucleus. This interaction, independent of autophagy, contributes to PML

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Oncology

Background:

  • The promyelocytic leukemia (PML) protein, often implicated in acute promyelocytic leukemia due to the PML-retinoic acid receptor alpha (RARα) fusion gene, can enhance autophagic activity.
  • PML overexpression leads to sequestration of microtubule-associated protein light chain 3 (LC3) within PML nuclear bodies, suggesting nuclear localization of LC3.
  • The functional significance of LC3's nucleoplasmic localization remains largely unknown.

Purpose of the Study:

  • To investigate the interaction between PML and LC3.
  • To determine the functional consequences of PML-LC3 interaction in cellular processes, particularly cell growth.
  • To explore the potential role of nuclear LC3 in tumor suppression.

Main Methods:

  • Co-immunoprecipitation (Co-IP) assays to assess protein interactions.
  • Co-localization studies using microscopy to visualize protein distribution.
  • Analysis of PML mutants lacking specific motifs to identify interaction regions.
  • Cell growth assays to evaluate the functional impact of the interaction.

Main Results:

  • PML and LC3 interact in a cell type-independent manner.
  • Overexpressed PML coprecipitates with endogenous and nuclear LC3.
  • PML-LC3 co-localization is enhanced by interferon-alpha (IFNα) induction and occurs during specific cell cycle phases (telophase and G1).
  • Two LC3-interacting region (LIR) motifs within PML are essential for LC3 binding, and this interaction is independent of autophagic activity.
  • The interaction between PML and LC3 contributes to PML's cell growth inhibitory function.

Conclusions:

  • PML directly interacts with LC3, including nuclear LC3, via specific LIR motifs.
  • This interaction is independent of canonical autophagic pathways.
  • The PML-LC3 interaction plays a role in suppressing cell growth.
  • Nuclear LC3 may function in conjunction with PML, a known tumor suppressor, to regulate cell growth and potentially inhibit cancer development.

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