PUBLICATION

A novel role for DYX1C1, a chaperone protein for both Hsp70 and Hsp90, in breast cancer

Authors
Chen, Y., Zhao, M., Wang, S., Chen, J., Wang, Y., Cao, Q., Zhou, W., Liu, J., Xu, Z., Tong, G., and Li, J.
ID
ZDB-PUB-100128-3
Date
2009
Source
Journal of Cancer Research and Clinical Oncology   135(9): 1265-1276 (Journal)
Registered Authors
Keywords
DYX1C1, Heat shock protein, Tetratricopeptide repeats, Protein interaction, Breast cancer
MeSH Terms
  • Molecular Sequence Data
  • Humans
  • Nerve Tissue Proteins/genetics
  • Nerve Tissue Proteins/metabolism*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Amino Acid Sequence
  • Up-Regulation/genetics
  • HSP70 Heat-Shock Proteins/metabolism*
  • Nuclear Proteins/genetics
  • Nuclear Proteins/metabolism*
  • Mutagenesis, Site-Directed
  • Female
  • HSP90 Heat-Shock Proteins/metabolism*
  • Breast Neoplasms/genetics
  • Breast Neoplasms/metabolism*
  • Breast Neoplasms/pathology
  • Two-Hybrid System Techniques
  • RNA, Messenger/genetics
PubMed
19277710 Full text @ J. Cancer Res. Clin. Oncol.
Abstract
AIMS: With three consecutive tetratricopeptide repeat (TPR) motifs at its C-terminus essential for neuronal migration, and a p23 domain at its N-terminus, DYX1C1 was the first gene proposed to have a role in developmental dyslexia. In this study, we attempted to identify the potential interaction of DYX1C1 and heat shock protein, and the role of DYX1C1 in breast cancer. MAIN METHODS: GST pull-down, a yeast two-hybrid system, RT-PCR, site-directed mutagenesis approach. KEY FINDINGS: Our study initially confirmed DYX1C1, a dyslexia related protein, could interact with Hsp70 and Hsp90 via GST pull-down and a yeast two-hybrid system. And we verified that EEVD, the C-terminal residues of DYX1C1, is responsible for the identified association. Further, DYX1C1 mRNA was significantly overexpressed in malignant breast tumor, linking with the up-regulated expression of Hsp70 and Hsp90. SIGNIFICANCE: These results suggest that DYX1C1 is a novel Hsp70 and Hsp90-interacting co-chaperone protein and its expression is associated with malignancy.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping