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C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis

Mark A Brown1, Kenneth Foreman2, June Harriss3

  • 1Department of Clinical Sciences, Colorado State University, Fort Collins, CO 80523, USA.

Oncotarget
|March 5, 2015
PubMed

Insights

The SMYD3 histone methyl transferase (HMTase) interacts with HSP90, a nuclear chaperone. This interaction is crucial for SMYD3

Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • SMYD3 histone methyl transferase (HMTase) and HSP90 are proto-oncogenes.
  • Their roles in human malignancies are independently established.

Purpose of the Study:

  • To investigate the interaction between SMYD3 and HSP90.
  • To elucidate the functional consequences of this interaction on SMYD3 activity and oncogenic potential.

Main Methods:

  • Co-immunoprecipitation assays to confirm physical interaction.
  • Site-directed mutagenesis to identify critical domains.
  • Cellular localization studies using microscopy.
  • Assessment of HMTase activity and cell proliferation assays.

Main Results:

  • A tetratricopeptide repeat (TPR)-like domain in SMYD3's C-terminal domain (CTD) mediates HSP90 binding.
  • SMYD3's CTD is essential for basal HMTase activity; the TPR-like structure is required for HSP90-enhanced activity.
  • Disruption of the SMYD3-HSP90 interaction causes SMYD3 mislocalization, loss of chromatin association, reduced cell proliferation, and potentially impaired oncogenic activity.

Conclusions:

  • The SMYD3-HSP90 interaction is critical for SMYD3's function and oncogenic activity.
  • Targeting this interaction offers a novel therapeutic strategy for SMYD3-overexpressing cancers.
  • This approach may provide a reduced toxicity profile compared to current HSP90 inhibitors.

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