Recruiting substrates to cullin 4-dependent ubiquitin ligases by DDB1.

Journal Article (Journal Article)

The ubiquitin-proteasome system is the major pathway by which cells target proteins for degradation in a specific manner. The E3 ubiquitin ligase, which brings targeted proteins (substrates) and activated ubiquitin in close proximity, enabling covalent conjugation of ubiquitin to the substrate, is an essential component of this system. Of the E3 ligases, the cullin (CUL) ligases are of high interest because of their capacity to form multiple distinct E3 complexes to ubiquitinate a potentially large number of substrates. Of the six closely related cullins, very little is known about how specific substrates are recruited to CUL4-dependent ligases. A recent paper in Nature Cell Biology may shed some light on this issue as well as on the function of DDB1, a damaged-DNA binding protein that has long been associated with DNA repair.

Full Text

Duke Authors

Cited Authors

  • McCall, CM; Hu, J; Xiong, Y

Published Date

  • January 2005

Published In

Volume / Issue

  • 4 / 1

Start / End Page

  • 27 - 29

PubMed ID

  • 15655366

Electronic International Standard Serial Number (EISSN)

  • 1551-4005

Digital Object Identifier (DOI)

  • 10.4161/cc.4.1.1396


  • eng

Conference Location

  • United States