Abstract
The novel protein p33MONOX (p33Monooxygenase) was over-expressed in neuroblastoma cells demonstrating its inhibitory effect on the phosphorylation of the App (amyloid precursor protein) and Bcl2 (B-cell lymphoma 2) proteins but mediating higher activation of Mapk1/3 (mitogen-activated protein kinase 1/3). We employed a variety of cell biology techniques to show the localization of p33MONOX to the cytoplasm of pyramidal neurons in the mouse brain hippocampus. We also carried out a yeast-two-hybrid screening plus co-immunoprecipitation and bio-informatics to determine COBRA1 (cofactor of BRCA1 (breast cancer type 1)), NOL12 (nucleolar protein 12), and PRNP (prion protein) as p33MONOX-interacting proteins. Bio-computational analyses revealed a flavine-containing monooxygenase (FMO)-1 motif, thus linking p33MONOX to a group of previously characterized proteins, the MICALs (molecule interacting with CasL). Concluding, p33MONOX might regulate pre- and post-transcriptional control of dynamic processes related to growth cone guidance.
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Acknowledgments
This study was supported by an A*STAR grant (BMRC/04/1/22/19/360) to K.H. We thank Ms H.J. Tang and S. Yusof (both from the School of Biological Sciences, Nanyang Technical University) for technical assistance. We are particularly grateful to Prof. Dr. R. Li (Department of Molecular Medicine, Institute of Biotechnology, The University of Texas Health Science Center, 15355 Lambda Drive, San Antonio, TX, 78245-3207, USA) for providing us the anti-COBRA1 antibody.
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Mishra, M., Inoue, N. & Heese, K. Characterizing the novel protein p33MONOX. Mol Cell Biochem 350, 127–134 (2011). https://doi.org/10.1007/s11010-010-0690-4
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DOI: https://doi.org/10.1007/s11010-010-0690-4