Ubiquitination-proteasome system: A new player in the pathogenesis of psoriasis and clinical implications

J Dermatol Sci. 2018 Mar;89(3):219-225. doi: 10.1016/j.jdermsci.2017.12.002. Epub 2017 Dec 13.

Abstract

Ubiquitination is an important post-translational modification that regulates a myriad of biological processes such as inflammation, immune response, cell differentiation and proliferation. During the last decade, progress in proteomics contributed to the identification of new E3 ligases and their substrates. Hence, deregulated ubiquitination events are found to be involved in several inflammatory disorders, exemplifying by systemic lupus erythematosus (SLE), type 1 diabetes, rheumatoid arthritis (RA) and psoriasis. Psoriasis is a chronic inflammatory skin disease characterized by epidermal hyperproliferation and differentiation. Through regulation of key transcriptional factors or signaling members, ubiquitination is viewed as a key regulator in psoriasis. Thus, targeting ubiquitination pathway holds potential for the treatment of psoriasis. Herein, we summarize the current understanding of ubiquitination in psoriasis, and discuss the prospects for targeting ubiquitination in the treatment of psoriasis.

Keywords: Proteasome; Psoriasis; Treatment; Ubiquitination.

Publication types

  • Review

MeSH terms

  • Forkhead Transcription Factors / physiology
  • Humans
  • NF-kappa B / physiology
  • Nuclear Receptor Subfamily 1, Group F, Member 3 / physiology
  • Proteasome Endopeptidase Complex / drug effects
  • Proteasome Endopeptidase Complex / physiology*
  • Psoriasis / drug therapy
  • Psoriasis / etiology*
  • Signal Transduction / physiology
  • Transforming Growth Factor beta / physiology
  • Ubiquitination*

Substances

  • FOXP3 protein, human
  • Forkhead Transcription Factors
  • NF-kappa B
  • Nuclear Receptor Subfamily 1, Group F, Member 3
  • RORC protein, human
  • Transforming Growth Factor beta
  • Proteasome Endopeptidase Complex