Journal of cancer research and clinical oncology · 2009
A novel role for DYX1C1, a chaperone protein for both Hsp70 and Hsp90, in breast cancer.
СтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Chen Yuxin, Zhao Muzi, Wang Saiqun, Chen Jie, Wang Yun, Cao Qinhong, Zhou Wenbin, Liu Jin, Xu Zhiyang, Tong Guoqing, Li Jianmin
Аннотация
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.
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.
Предметные рубрики MeSH
Amino Acid SequenceBreast NeoplasmsCytoskeletal ProteinsFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNuclear ProteinsRNA, MessengerReverse Transcriptase Polymerase Chain ReactionTwo-Hybrid System TechniquesUp-Regulation