Hyperphosphlorylated p107 and p130 bind to T-antigen: Identification of a critical regulatory sequence present in RE but not in p107/p130

Erik S. Knudsen, Jean Y J Wang

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The retinoblastoma tumor suppressor RB and its related proteins, p107 and p130, are targets of several viral oncoproteins, including SV40 large T-antigen (T-Ag) and adenovirus E1A. T-Ag and LXCXE-peptide motif through which binding to the conserved 'A/B pocket' present in RE, p107 and p130 is achieved. The LXCSE-binding activity of RB, we have previously shown, is inhibited by phosphorylation at Thr 821 and 826 in the C-terminal region of RB. Thr 821 and its surrounding sequence is unique to RB and not found in p107 or p130, Interestingly, hyperphosphorylation of p107 does not disrupt its ability to bind T-Ag or to inhibit the transactivating function of E1A. Insertion of a fourteen amino acid sequence of RB containing Thr 821 into p107 prevents binding of T-Ag and E1A to phosphorylated p107, These results show that the RE sequence surrounding Thr 821 plays a critical role in the regulation of the 'A/B pocket' function, In addition, these data indicate that the protein binding functions of RB and p107 are not equivalently regulated by phosphorylation.

Original languageEnglish (US)
Pages (from-to)1655-1663
Number of pages9
JournalOncogene
Volume16
Issue number13
StatePublished - Apr 2 1998

Fingerprint

Viral Tumor Antigens
Phosphorylation
Polyomavirus Transforming Antigens
Retinoblastoma
Oncogene Proteins
Protein Binding
Adenoviridae
Amino Acid Sequence
Peptides
Neoplasms
Proteins

Keywords

  • Cell cycle
  • E2f-1:
  • E2f4:
  • Eia
  • Tumor suppressor

ASJC Scopus subject areas

  • Cancer Research
  • Genetics
  • Molecular Biology

Cite this

Hyperphosphlorylated p107 and p130 bind to T-antigen : Identification of a critical regulatory sequence present in RE but not in p107/p130. / Knudsen, Erik S.; Wang, Jean Y J.

In: Oncogene, Vol. 16, No. 13, 02.04.1998, p. 1655-1663.

Research output: Contribution to journalArticle

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