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12:19
Three-Dimensional (3D) Tumor Spheroid Invasion Assay
Published on: May 1, 2015
Copine-III interacts with ErbB2 and promotes tumor cell migration.
C Heinrich1, C Keller, A Boulay
1Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Oncogene
|December 17, 2009
Summary
Copine-III binds to ErbB2 in breast cancer cells, impacting cell motility. This protein may play a role in various cancers, correlating with ERBB2 amplification in breast tumors.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- ErbB2 amplification is linked to aggressive breast cancer and poor prognosis.
- Identifying novel ErbB2-interacting proteins is crucial for understanding cancer progression.
Purpose of the Study:
- To identify novel proteins interacting with ErbB2.
- To investigate the role of Copine-III in ErbB2-mediated signaling and cancer cell motility.
Main Methods:
- Stable isotope labeling of amino acids in cell culture (SILAC) followed by peptide affinity pull-downs.
- Mass spectrometry for relative quantification of protein binders.
- Analysis of Copine-III expression in breast, prostate, and ovarian tumors.
Main Results:
- Copine-III was identified as a novel binding partner of phosphorylated Tyr1248 of ErbB2.
- Copine-III requires Ca(2+) for plasma membrane binding and interacts with ErbB2 upon stimulation.
- Copine-III knockdown reduces Src kinase activation and ErbB2-dependent wound healing in breast cancer cells.
- High CPNE3 RNA levels correlate with ERBB2 amplification in primary breast tumors.
- Differential protein expression of Copine-III observed in normal versus tumor tissues.
Conclusions:
- Copine-III is a novel regulator of ErbB2-dependent cancer cell motility.
- Copine-III may have a broader role in carcinogenesis across multiple cancer types.
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