Skip to main content
Log in

Polyubiquitin chains: functions, structures, and mechanisms

  • Review
  • Published:
Cellular and Molecular Life Sciences Aims and scope Submit manuscript


Ubiquitin is a highly conserved 76-aminoacid polypeptide that is found throughout the eukaryotic kingdom. The covalent conjugation of ubiquitin (often in the form of a polymer) to substrates governs a variety of biological processes ranging from proteolysis to DNA damage tolerance. The functional flexibility of this post-translational modification has its roots in the existence of a large number of ubiquitinating enzymes that catalyze the formation of distinct ubiquitin polymers, which in turn encode different signals. This review summarizes recent advances in the field with an emphasis on the non-canonical functions of polyubiquitination. We also discuss the potential mechanism of chain linkage specification as well as how structural disparity in ubiquitin polymers may be distinguished by ubiquitin receptors to translate the versatile ubiquitin signals into various cellular functions.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Author information

Authors and Affiliations


Corresponding author

Correspondence to Y. Ye.

Additional information

Received 20 February 2008; received after revision 12 March 2008; accepted 1 April 2008

Rights and permissions

Reprints and permissions

About this article

Cite this article

Li, W., Ye, Y. Polyubiquitin chains: functions, structures, and mechanisms. Cell. Mol. Life Sci. 65, 2397–2406 (2008).

Download citation

  • Published:

  • Issue Date:

  • DOI: