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Annexin A2 is a novel RNA-binding protein
Nolan R Filipenko1, Travis J MacLeod, Chang-Soon Yoon
1Cancer Biology Research Group, Departments of Biochemistry & Molecular Biology and Oncology, University of Calgary, Calgary, Alberta T2N 4N1, Canada.
The Journal of Biological Chemistry
|December 16, 2003
Summary
Annexin A2 (ANXA2), a calcium-dependent protein, directly binds to c-myc mRNA. This interaction up-regulates c-Myc protein, suggesting ANXA2
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Annexin A2 (ANXA2) is a calcium-binding protein implicated in viral transformations and human tumors.
- Its role in RNA binding and oncogene regulation is not fully understood.
Purpose of the Study:
- To investigate the direct interaction between Annexin A2 (ANXA2) and human c-myc RNA.
- To determine the functional consequence of ANXA2 binding to c-myc mRNA in cellular systems.
Main Methods:
- In vitro binding assays using ribonucleotide homopolymers and c-myc RNA.
- Immunoprecipitation and reverse transcriptase-PCR from HeLa cells to identify in vivo interactions.
- Sucrose gradient analysis to determine ANXA2 association with ribonucleoprotein complexes.
- Cell transfection studies to assess c-Myc protein levels.
Main Results:
- ANXA2 specifically binds to poly(G) RNA with high affinity (Kd = 60 nM) in a calcium-dependent manner.
- ANXA2 forms ribonucleoprotein complexes in vivo, associating with c-myc mRNA.
- ANXA2 interaction with c-myc mRNA leads to increased c-Myc protein levels in transfected cells.
Conclusions:
- ANXA2 is identified as a calcium-dependent RNA-binding protein.
- ANXA2 directly interacts with c-myc mRNA, suggesting a role in regulating this nuclear oncogene.
- ANXA2 may contribute to oncogenesis through modulation of c-Myc expression.