Signal integration and diversification through the p62 scaffold protein

Trends Biochem Sci. 2007 Feb;32(2):95-100. doi: 10.1016/j.tibs.2006.12.002. Epub 2006 Dec 15.

Abstract

Signal specificity of multifunctional enzymes is achieved through protein-protein interactions involving specific domains on scaffold proteins. p62 (also known as sequestosome 1) is such a scaffold protein that possesses PB1 and UBA domains, and the TRAF6 binding sequence. Proteins recruited to these domains enable p62 to integrate kinase-activated and ubiquitin-mediated signaling pathways. The biological function of p62 has been studied in diverse systems and processes such as osteoclastogenesis, inflammation, differentiation, neurotrophin biology and obesity. The availability of mice in which p62 has been genetically inactivated is providing new insight into the mechanism and function of p62 at a whole-organism level.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism*
  • Carrier Proteins / metabolism*
  • Humans
  • NF-kappa B / metabolism
  • Nuclear Proteins / metabolism
  • Sequestosome-1 Protein
  • Signal Transduction*
  • TNF Receptor-Associated Factor 6 / metabolism
  • Transcription Factors / metabolism
  • Ubiquitin / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • NF-kappa B
  • Nuclear Proteins
  • PBRM1 protein, human
  • SQSTM1 protein, human
  • Sequestosome-1 Protein
  • TNF Receptor-Associated Factor 6
  • Transcription Factors
  • Ubiquitin