Send to

Choose Destination
Biochem Biophys Res Commun. 2009 Nov 20;389(3):506-11. doi: 10.1016/j.bbrc.2009.09.011. Epub 2009 Sep 6.

ZNRF1 interacts with tubulin and regulates cell morphogenesis.

Author information

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


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.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science Icon for Hokkaido University Collection of Scholarly and Academic Papers: HUSCAP
Loading ...
Support Center