Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus

Nat Cell Biol. 2002 Feb;4(2):106-10. doi: 10.1038/ncb740.

Abstract

Promyelocytic leukaemia (PML) nuclear bodies are present in most mammalian cell nuclei. PML bodies are disrupted by PML retinoic acid receptor alpha (RAR alpha) oncoproteins in acute promyelocytic leukaemia. These bodies contain numerous proteins, including Sp100, SUMO-1, HAUSP(USP7), CBP and BLM, and they have been implicated in aspects of transcriptional regulation or as nuclear storage depots. Here, we show that three classes of PML nuclear bodies can be distinguished, on the basis of their dynamic properties in living cells. One class of PML bodies is particularly noteworthy in that it moves by a metabolic-energy-dependent mechanism. This represents the first example of metabolic-energy-dependent transport of a nuclear body within the mammalian cell nucleus.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, Nuclear*
  • Autoantigens / genetics
  • Autoantigens / metabolism
  • Bacterial Proteins / metabolism
  • Cell Line
  • Cell Nucleus / metabolism*
  • Cricetinae
  • Energy Metabolism*
  • Humans
  • Leukemia, Promyelocytic, Acute / physiopathology
  • Luminescent Proteins / metabolism
  • Microscopy, Fluorescence
  • Models, Biological
  • Movement
  • Myosins / antagonists & inhibitors
  • Neoplasm Proteins / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Oncogene Proteins, Fusion / metabolism*
  • Promyelocytic Leukemia Protein
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Time Factors
  • Transcription Factors / metabolism*
  • Tumor Suppressor Proteins

Substances

  • Antigens, Nuclear
  • Autoantigens
  • Bacterial Proteins
  • Luminescent Proteins
  • Neoplasm Proteins
  • Nuclear Proteins
  • Oncogene Proteins, Fusion
  • Promyelocytic Leukemia Protein
  • Recombinant Fusion Proteins
  • Transcription Factors
  • Tumor Suppressor Proteins
  • promyelocytic leukemia-retinoic acid receptor alpha fusion oncoprotein
  • yellow fluorescent protein, Bacteria
  • SP100 protein, human
  • PML protein, human
  • Myosins