A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination

Jing Yan, Di Zhang, Yujun Di, Huili Shi, Hai Rao, Keke Huo

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The SCY1-like 1 binding protein 1 (SCYL1-BP1) protein was identified as an interacting partner of E3 ligase p53-induced RING H2 protein (Pirh2) and mouse double minute gene number 2 (MDM2) by yeast two-hybrid screening. Further investigation suggested there are two interactions involved in different mechanisms. SCYL1-BP1 can be ubiquitinated and degraded by Pirh2 but not by MDM2, which suggests that SCYL1-BP1 can be regulated by Pirh2. On the other hand, while SCYL1-BP1 binds to ubiquitin E3 ligase MDM2, it promotes MDM2 self-ubiquitination and results in a reduction of MDM2 protein level.

Original languageEnglish (US)
Pages (from-to)3275-3278
Number of pages4
JournalFEBS Letters
Volume584
Issue number15
DOIs
StatePublished - Aug 2010

Fingerprint

Ubiquitination
Carrier Proteins
Genes
Substrates
Ubiquitin-Protein Ligases
Proteins
Yeast
Screening
Yeasts

Keywords

  • Mouse double minute gene number 2
  • P53-Induced RING H2 protein
  • Protein degradation
  • SCY1-like 1 binding protein 1
  • Ubiquitination

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination. / Yan, Jing; Zhang, Di; Di, Yujun; Shi, Huili; Rao, Hai; Huo, Keke.

In: FEBS Letters, Vol. 584, No. 15, 08.2010, p. 3275-3278.

Research output: Contribution to journalArticle

Yan, Jing ; Zhang, Di ; Di, Yujun ; Shi, Huili ; Rao, Hai ; Huo, Keke. / A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination. In: FEBS Letters. 2010 ; Vol. 584, No. 15. pp. 3275-3278.
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AU - Rao, Hai

AU - Huo, Keke

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