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Interaction between the pRb2/p130 C-terminal domain and the N-terminal portion of cyclin D3

✍ Scribed by Francesco Bonetto; Maurizio Fanciulli; Tullio Battista; Antonio De Luca; Patrizia Russo; Tiziana Bruno; Roberta De Angelis; Monica Di Padova; Antonio Giordano; Armando Felsani; Marco G. Paggi

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 222 KB
Volume: 75
Category: Article
ISSN: 0730-2312
DOI: 10.1002/(sici)1097-4644(19991215)75:4<698::aid-jcb15>3.0.co;2-7

No coin nor oath required. For personal study only.

✦ Synopsis

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.

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