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

Francesco Bonetto, Maurizio Fanciulli, Tullio Battista, Antonio De Luca, Patrizia Russo, Tiziana Bruno, Roberta De Angelis, Monica Di Padova, Antonio Giordano, Armando Felsani, Marco C. Paggi

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)698-709
Number of pages12
JournalJournal of Cellular Biochemistry
Volume75
Issue number4
DOIs
Publication statusPublished - Dec 15 1999

Keywords

  • Cell cycle
  • Cyclin D3
  • Differentiation
  • Phosphorylation
  • Protein-protein interaction
  • Rb2/p130

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'Interaction between the pRb2/p130 C-terminal domain and the N-terminal portion of cyclin D3'. Together they form a unique fingerprint.

  • Cite this