The relative cellular levels of CP2a and CP2b potentiates erythroid cell-specific expression of the alpha-globin gene by regulating the nuclear localization of CP2c
- Authors
- Chae, Ji Hyung; Kang, Ho Chul; Kim, Chul Geun
- Issue Date
- Mar-2009
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Subcellular localization; Protein protein interaction; Transcription factor complex; CP2b; CP2c; alpha-Globin gene
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.380, no.4, pp.813 - 817
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 380
- Number
- 4
- Start Page
- 813
- End Page
- 817
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/177201
- DOI
- 10.1016/j.bbrc.2009.01.172
- ISSN
- 0006-291X
- Abstract
- CP2b activates alpha-globin expression in an erythroid cell-specific manner, through interaction with CP2c and PIAS1. Although CP2a is identical to CP2b except for lacking an exon encoding additional 36 amino acids and has the intrinsic DNA binding and transactivation properties, it does not exert any role in alpha-globin expression. Investigation of subcellular localization of exogenous CP2 proteins revealed that CP2a and CP2b were exclusively localized in the cytosol and nucleus, respectively. The CP2b-specific exon was in charge of the nuclear localization of CP2b. Interestingly, subcellular localization of CP2c was either in the nucleus or cytosol depending on the relative level of CP2a and CP2b although CP2c intrinsically localized in the cytosol in the absence of CP2a/CP2b. Finally, dramatic increment of hemoglobin expression was correlated with nuclear translocation of CP2c during MEL cell differentiation. Our data suggest that CP2b potentiate erythroid cell-specific alpha-globin expression by recruiting CP2c into the nucleus.
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