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Updated: Mar 11, 2026

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
Published on: March 3, 2016
Centromere protein W interacts with beta-transducin repeat-containing protein 1 and modulates its subcellular
Yeongmi Cheon1, Seyeong Jeon1, Soojin Lee1
1Department of Microbiology and Molecular Biology, Chungnam National University, Daejeon, Korea.
Abstract:
Beta-transducin repeat-containing protein 1 (β-TrCP1) is a substrate-recognition module of SCFβ-TrCP1 ubiquitin ligases and its subcellular distribution is known to be critical for target specificity. Heterogeneous nuclear ribonucleoprotein (hnRNP) U, an abundant nuclear protein, is known to be a unique regulator of β-TrCP1 shuttling between the cytoplasm and the nucleus. In this study, we report that centromere protein W (CENP-W), which is frequently overexpressed in a variety of human cancers, may also contribute to β-TrCP1 shuttling. Although hnRNP U and CENP-W can interact with β-TrCP1 and transport it independently, these proteins do not compete for β-TrCP1 binding, but rather cooperate to form a stable shuttling complex. Intriguingly, we found that overexpression of CENP-W leads to accumulation of β-TrCP1 in the nucleus. Thus, we propose that CENP-W may function as a booster of β-TrCP1 nuclear import to increase the oncogenicity of β-TrCP1.
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