Chibby interacts with NBPF1 and clusterin, two candidate tumor suppressors linked to neuroblastoma.

The NBPF genes are members of a gene family that underwent a remarkable increase in their copy number during recent primate evolution. The NBPF proteins contain 5 to 40 copies of a domain known as the NBPF repeat or DUF1220. Very little is known about the function of these domains ...
or about the NBPF proteins. We performed a yeast two-hybrid screening with the aminoterminal domain of NBPF11 and found that Chibby, a documented repressor of Wnt signaling, interacts with multiple NBPF proteins. More specifically, a coiled-coil region in the NBPF proteins interacts with the coiled-coil domain in the carboxyterminal region of Chibby. Nonetheless, this interaction did not influence the repressor function of Chibby in a TOPFLASH reporter assay. Using Chibby as bait in a new yeast two-hybrid screening, we identified clusterin as a binding protein. Chibby and clusterin were co-immunoprecipitated with NBPF1, suggesting the formation of a tri-molecular complex. Although we have not pinpointed the role of these mutual interactions, the possible formation of a macromolecular complex of three candidate tumor suppressor proteins, including the enigmatic NBPF1, points at important functional implications.
Mesh Terms:
Carrier Proteins, Cells, Cultured, Clusterin, HeLa Cells, Humans, Immunoprecipitation, Models, Biological, Neoplasm Proteins, Neuroblastoma, Nuclear Proteins, Protein Binding, Protein Interaction Domains and Motifs, Protein Transport, Signal Transduction, Tissue Distribution, Tumor Suppressor Proteins, Wnt Proteins
Exp. Cell Res.
Date: Apr. 15, 2010
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