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The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link

Z Topcu1, D L Mack, R A Hromas

  • 1Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029, USA.

Oncogene
|December 22, 1999
PubMed

Insights

Researchers discovered that the promyelocytic leukemia protein (PML) and protein Z bind the proline-rich homeodomain protein (PRH). This interaction may link cell growth control and hematopoiesis in leukemia.

Area of Science:

  • Molecular Biology
  • Hematology
  • Cell Biology

Background:

  • Acute promyelocytic leukemia (APL) involves disrupted myeloid cell differentiation due to chromosomal translocations affecting the PML protein and its nuclear bodies.
  • Disruption of PML and its nuclear bodies is associated with loss of growth control and leukemogenesis.

Purpose of the Study:

  • To identify protein partners of PML and Z, specifically focusing on their interaction with the proline-rich homeodomain protein (PRH).
  • To investigate the functional implications of the PML-PRH interaction in hematopoiesis and cell growth control.

Main Methods:

  • Yeast two-hybrid assays were employed to identify protein-protein interactions.
  • Immunoprecipitation and co-localization studies were performed in K562 and NB4 cell lines.

Main Results:

  • PML and Z were found to bind PRH via their RING domains, identifying them as the first reported protein partners for PRH.
  • PML and PRH were observed to interact in both K562 and NB4 cell lines, with PRH exhibiting a punctate distribution in the nucleus and cytoplasm.

Conclusions:

  • The interaction between PML and PRH, involving PML's RING domain and PRH's repressor domain, suggests a novel link between cell growth regulation and hematopoietic processes.
  • This finding offers potential insights into the mechanisms underlying leukemogenesis, particularly in APL.

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