| First Author | Ling YH | Year | 2014 |
| Journal | Exp Cell Res | Volume | 327 |
| Issue | 1 | Pages | 12-23 |
| PubMed ID | 24858563 | Mgi Jnum | J:217575 |
| Mgi Id | MGI:5614551 | Doi | 10.1016/j.yexcr.2014.05.008 |
| Citation | Ling YH, et al. (2014) CCHCR1 interacts with EDC4, suggesting its localization in P-bodies. Exp Cell Res 327(1):12-23 |
| abstractText | Coiled-coil alpha-helical rod protein 1 (CCHCR1) is suggested as a candidate biomarker for psoriasis for more than a decade but its function remains poorly understood because of the inconsistent findings in the literature. CCHCR1 protein is suggested to be localized in the cytoplasm, nucleus, mitochondria, or centrosome and to regulate various cellular functions, including steroidogenesis, proliferation, differentiation, and cytoskeleton organization. In this study, we attempted to find a consensus between these findings by identifying the interaction partners of CCHCR1 using co-immunoprecipiation with a stable cell line expressing EGFP-tagged CCHCR1. Out of more than 100 co-immunoprecipitants identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS), the enhancer of mRNA-decapping protein 4 (EDC4), which is a processing body (P-body) component, was particularly found to be the major interacting partner of CCHCR1. Confocal imaging confirmed the localization of CCHCR1 in P-bodies and its N-terminus is required for this subcellular localization, suggesting that CCHCR1 is a novel P-body component. As P-bodies are the site for mRNA metabolism, our findings provide a molecular basis for the function of CCHCR1, any disruption of which may affect the transcriptome of the cell, and causing abnormal cell functions. |
