Amphiphysin IIb-1, a novel splicing variant of amphiphysin II, regulates p73 beta function through protein-protein interactions
- Authors
- Kim, KC; Kim, TS; Kang, KH; Choi, KH
- Issue Date
- 11-Oct-2001
- Publisher
- NATURE PUBLISHING GROUP
- Keywords
- p73; amphiphysin IIb-1; SH3 domain; NLS; yeast two-hybrid; splicing variants
- Citation
- ONCOGENE, v.20, no.46, pp 6689 - 6699
- Pages
- 11
- Journal Title
- ONCOGENE
- Volume
- 20
- Number
- 46
- Start Page
- 6689
- End Page
- 6699
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/47225
- DOI
- 10.1038/sj.onc.1204839
- ISSN
- 0950-9232
1476-5594
- Abstract
- p73 is a nuclear protein that is similar in structure and function to p53. Notably, the C-terminal region of p73 has a regulatory function, through interactions with a positive or negative regulator. In this study, we use the yeast two-hybrid technique to identify a novel p73 beta binding protein, designated amphiphysin IIb-1. Amphiphysin IIb-1 is one of the splicing variants of amphiphysin II, and has a shorter protein product than amphiphysin IIb, which has been previously reported. We confirmed that amphiphysin IIb-1 binds full-length p73 beta, both in vitro and in vivo. This association is mediated via the SH3 domain of amphiphysin IIb-1 and C-terminal amino acids 321-376 of p73 beta. Double immunofluorescence patterns revealed that p73 beta is relocalized to the cytoplasm in the presence of amphiphysin IIb-1. Overexpression of amphiphysin IIb-1 was found to significantly inhibit the transcriptional activity of p73 beta in a dose-dependent manner. In addition, the cell death function of p73 beta was inhibited by amphiphysin IIb-1. These findings offer a new insight into the regulation mechanism of p73 beta, and suggest that amphiphysin IIb-1 modulates p73 beta function by direct binding.
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