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Gene Review

Rbbp6  -  retinoblastoma binding protein 6

Mus musculus

Synonyms: 4933422O15Rik, AI316869, BB233631, C030034J04Rik, C77662, ...
 
 
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Disease relevance of Rbbp6

  • In association with mitotic apoptosis, P2P-R protein appears to dissociate from the periphery of chromosomes and localize in the cytoplasm and in cell surface blebs [1].
 

High impact information on Rbbp6

  • Evidence that the P2P-R cDNA encodes a protein domain that binds Rb1 was established using a glutathione S-transferase fusion protein to selectively precipitate Rb1 from cellular extracts [2].
  • The current studies were performed to evaluate if overexpression of specific segments of the P2P-R protein promote apoptosis in human MCF-7 cells that contain p53 and employ a different apoptotic signaling pathway [3].
  • Therefore, P2P-R-promoted apoptosis induced by camptothecin may be influenced by such interactions [3].
  • Since segments of P2P-R were found not to induce apoptosis independently, the ability of three different P2P-R segments to promote camptothecin-induced apoptosis was evaluated following their stable transfection and expression in MCF-7 cells [3].
  • The stable overexpression of near full-length P2P-R protein in human Saos 2 cells restricts cell cycle progression by inducing mitotic arrest at prometaphase and mitotic apoptosis (Gao and Scott, 2002) [3].
 

Biological context of Rbbp6

  • These results establish that the P2P-R cDNA encodes protein domains involved in both hnRNP association and Rb1 binding and complement recent reports that localize Rb1 to sites of RNA processing in the nucleus [2].
  • These findings suggest that P2P-R might serve a functional role in mitosis [1].
  • P2P-R protein overexpression restricts mitotic progression at prometaphase and promotes mitotic apoptosis [1].
 

Anatomical context of Rbbp6

  • MATERIALS AND METHODS: The ability of the microtubule disruption drug nocodazole to induce mitotic arrest and the ability of UV irradiation to induce apoptosis was evaluated in native versus cells made P2P-R deficient by P2P-R antisense treatment [4].
 

Associations of Rbbp6 with chemical compounds

 

Other interactions of Rbbp6

  • Those effects of P2P-R were observed in Saos-2 cells that lack p53 and employ a caspase-3-dependent apoptotic signaling pathway [3].
  • The proliferation potential protein-related (P2P-R) gene with domains encoding heterogeneous nuclear ribonucleoprotein association and Rb1 binding shows repressed expression during terminal differentiation [2].
  • During mitosis, the distribution of P2P-R protein also changes from a primary nucleolar localization in interphase cells to the periphery of chromosome in mitotic cells [1].
 

Analytical, diagnostic and therapeutic context of Rbbp6

References

 
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