DEPTOR ubiquitination and destruction by SCF β-TrCP

Zhiwei Wang, Jiateng Zhong, Daming Gao, Hiroyuki Inuzuka, Pengda Liu, Wenyi Wei

Research output: Contribution to journalReview articlepeer-review

14 Citations (Scopus)

Abstract

β-Transducin repeats-containing protein (β-TrCP) is the substrate recognition subunit of the SCF (SKP1, CUL1, and F-box protein)-type E3 ubiquitin ligase complex. SCF β-TrCP ubiquitinates specifically phosphorylated substrates to promote their subsequent destruction by the 26S proteasome and plays a critical role in various human diseases including tumorigenesis. We and others (Duan S et al. Mol Cell 44: 317-324, 2011; Gao D et al. Mol Cell 44: 290-303, 2011; Zhao Y et al. Mol Cell 44: 304-316, 2011) recently reported that SCF β-TrCP regulates cell growth and autophagy by controlling the ubiquitination and destruction of DEPTOR, an endogenous mammalian target of rapamycin inhibitor, in a phosphorylation-dependent manner. In this review, we discuss β-TrCP's new downstream substrate, DEPTOR, as well as summarize the novel functional aspects of β-TrCP in controlling cell growth and regulating autophagy, in part through governing the stability of DEPTOR.

Original languageEnglish
Pages (from-to)E163-E169
JournalAmerican Journal of Physiology - Endocrinology and Metabolism
Volume303
Issue number2
DOIs
Publication statusPublished - 2012 Jul 15
Externally publishedYes

Keywords

  • Cancer
  • Mammalian target of rapamycin
  • Skp1- Cullin1-F-box protein
  • β-transducin repeats-containing protein

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Physiology
  • Physiology (medical)

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