ZNRF1 interacts with tubulin and regulates cell morphogenesis.

Koichi Yoshida, Masashi Watanabe, Shigetsugu Hatakeyama

Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, Japan.

Biochemical and biophysical research communications 2009 Nov 20

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The ubiquitin-proteasome system has been implicated in neuronal degeneration and regeneration. We demonstrated that overexpression of ZNRF1, which has been identified as a crucial molecule in nerve regeneration, causes morphological changes such as neurite-like elongation. Molecular dissections showed that both the RING finger domain and zinc finger domain are required for morphological changes. Furthermore, we identified beta-tubulin type 2 (Tubb2) as a ZNRF1-binding protein by yeast two-hybrid screening. In vivo binding assay showed that ZNRF1 interacts with Tubb2 and immunofluorescent staining suggests that ZNRF1 is colocalized with Tubb2. These results suggest that ZNRF1 mediates regulation of neuritogenesis via interaction with tubulin.

Citation

Koichi Yoshida, Masashi Watanabe, Shigetsugu Hatakeyama. ZNRF1 interacts with tubulin and regulates cell morphogenesis. Biochemical and biophysical research communications. 2009 Nov 20;389(3):506-11