An association between cyclin D3 and the C-terminal domain of pRb2/p130 was demonstrated using the yeast two-hybrid system. Further analysis restricted the epitope responsible for the binding within the 74 N-terminal amino acids of cyclin D3, independent of the LXCXE amino acid motif present in the D-type cyclin N-terminal region. In a coprecipitation assay in T98G cells, a human glioblastoma cell line, the C-terminal domain of pRb2/p130 was able to interact solely with cyclin D3, while the corresponding portion of pRb interacted with either cyclin D3 or cyclin D1. In T98G cells, endogenous cyclin D3-associated kinase activity showed a clear predisposition to phosphorylate preferentially the C-terminal domain of pRb2/p130, rather than that of pRb. This propensity was also confirmed in LAN-5 human neuroblastoma cells, where phosphorylation of the pRb2/p130 C-terminal domain and expression of cyclin D3 also decreased remarkably in the late neural differentiation stages.

Bonetto, F., Fanciulli, M., Battista, T., DE LUCA, A., Russo, P., Bruno, C., et al. (1999). Interaction between the Rb2/p130 C-terminal domain and the N-terminal portion of cyclin D3. JOURNAL OF CELLULAR BIOCHEMISTRY, 75(4), 698-709 [10.1002/(SICI)1097-4644(19991215)75:4<698::AID-JCB15>3.0.CO;2-7].

Interaction between the Rb2/p130 C-terminal domain and the N-terminal portion of cyclin D3

GIORDANO, ANTONIO;
1999-01-01

Abstract

An association between cyclin D3 and the C-terminal domain of pRb2/p130 was demonstrated using the yeast two-hybrid system. Further analysis restricted the epitope responsible for the binding within the 74 N-terminal amino acids of cyclin D3, independent of the LXCXE amino acid motif present in the D-type cyclin N-terminal region. In a coprecipitation assay in T98G cells, a human glioblastoma cell line, the C-terminal domain of pRb2/p130 was able to interact solely with cyclin D3, while the corresponding portion of pRb interacted with either cyclin D3 or cyclin D1. In T98G cells, endogenous cyclin D3-associated kinase activity showed a clear predisposition to phosphorylate preferentially the C-terminal domain of pRb2/p130, rather than that of pRb. This propensity was also confirmed in LAN-5 human neuroblastoma cells, where phosphorylation of the pRb2/p130 C-terminal domain and expression of cyclin D3 also decreased remarkably in the late neural differentiation stages.
1999
Bonetto, F., Fanciulli, M., Battista, T., DE LUCA, A., Russo, P., Bruno, C., et al. (1999). Interaction between the Rb2/p130 C-terminal domain and the N-terminal portion of cyclin D3. JOURNAL OF CELLULAR BIOCHEMISTRY, 75(4), 698-709 [10.1002/(SICI)1097-4644(19991215)75:4<698::AID-JCB15>3.0.CO;2-7].
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/11065
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo