Abstract
The expression of the nuclear protein Ki-67 (pKi-67) is strictly correlated with cell proliferation. Because of this, anti-Ki-67 antibodies can be used as operational markers to estimate the growth fraction of human neoplasia in situ. For a variety of tumours, the assessment of pKi-67 expression has repeatedly been proven to be of prognostic value for survival and tumour recurrence, but no cellular function has yet been ascribed to the Ki-67 protein. This study shows that a C-terminal domain of pKi-67 (Kon21) is able to bind to all three members of the mammalian heterochromatin protein 1 (HP1) family in vitro and in vivo. This interaction can be manipulated in living cells, as evidenced by ectopic expression of GFP-tagged HP1 proteins in HeLa cells, which results in a dramatic relocalization of endogenous pKi-67. Taken together, the data presented in this study suggest a role for pKi-67 in the control of higher-order chromatin structure.
Original language | English |
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Pages (from-to) | 135-44 |
Number of pages | 10 |
Journal | Journal of Pathology |
Volume | 196 |
Issue number | 2 |
DOIs | |
Publication status | Published - Feb 2002 |
Keywords
- Animals
- Cell Division
- Cell Nucleus
- Chromatin
- Chromosomal Proteins, Non-Histone
- Fluorescent Antibody Technique
- Green Fluorescent Proteins
- HeLa Cells
- Humans
- Interphase
- Ki-67 Antigen
- Luminescent Proteins
- Protein Isoforms
- Recombinant Fusion Proteins
- Transfection
- Two-Hybrid System Techniques
- Journal Article
- Research Support, Non-U.S. Gov't