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

• P2P-R deficiency modifies nocodazole-induced mitotic arrest and UV-induced apoptosis [4].

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

• Confocal microscopy further established that 85% of the mitotic cell population had prometaphase characteristics suggesting that P2P-R overexpression restricts mitotic progression at prometaphase [1].
• The presence of P2P-R in cell surface blebs was confirmed by analysis of highly enriched populations of apoptotic cell surface blebs wherein Western blotting documented the presence of 250 kDa P2P-R [1].

References