TRIM36 interacts with the kinetochore protein CENP-H and delays cell cycle progression

Naoto Miyajima1, Satoru Maruyama, Katsuya Nonomura

  • 1Department of Biochemistry, Hokkaido University Graduate School of Medicine, N15, W7, Kita-ku, Sapporo, Hokkaido 060-8638, Japan.

The tripartite motif-containing protein (TRIM) family is defined by the presence of a common domain structure composed of a RING finger, a B-box, and a coiled-coil motif. TRIM family proteins are involved in a broad range of biological processes and, consistently, their alterations result in diverse pathological conditions such as genetic diseases, viral infection, and cancer development. In this study, we found by using yeast two-hybrid screening that TRIM36 has a ubiquitin ligase activity and interacts with centromere protein-H, one of the kinetochore proteins. We also found by immunofluorescence analysis that TRIM36 colocalizes with alpha-tubulin, one of the microtubule proteins. Moreover, we found that overexpression of TRIM36 decelerates the cell cycle and attenuates cell growth. These results indicate that TRIM36 is potentially associated with chromosome segregation and that an excess of TRIM36 may cause chromosomal instability.

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