p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners

Helen Rizos*, Sarah Woodruff, Richard F. Kefford

*Corresponding author for this work

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

The p14ARF tumour suppressor regulates a series of cell cycle regulatory proteins to promote cell cycle arrest in response to abnormal hyperproliferative growth stimuli. p14ARF alterations are common in human cancers and, when inherited, confer susceptibility to cutaneous melanoma. We now propose that the mechanism of p14ARF action may involve the covalent modification of its binding partners with the small ubiquitin-related protein SUMO-1. In particular, we demonstrate that p14ARF interacts with the SUMO E2 conjugating enzyme, Ubc9 and enhances the sumoylation of its binding partners, hdm2, E2F-1, HIF-1α, TBP-1 and p120E4F. Furthermore, p14ARF-induced sumoylation is abrogated by a subset of melanoma-associated p14ARF mutations. These results provide a mechanism for p14ARF action through a common modification of diverse binding partners.

Original languageEnglish
Pages (from-to)597-603
Number of pages7
JournalCell Cycle
Volume4
Issue number4
Publication statusPublished - 2005
Externally publishedYes

Keywords

  • hdm2
  • Melanoma
  • p14
  • Sumoylation

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