Ubiquitin ligation without a ligase

Mark Hochstrasser

doi:10.1016/j.devcel.2007.06.003

Ubiquitin ligation without a ligase

Dev Cell. 2007 Jul;13(1):4-6. doi: 10.1016/j.devcel.2007.06.003.

Author

Mark Hochstrasser¹

Affiliation

¹ Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu

PMID: 17609103
DOI: 10.1016/j.devcel.2007.06.003

Abstract

Classically, ubiquitination requires three enzymes acting in sequence: E1, E2, and E3. E3 ubiquitin ligases typically provide substrate specificity. An article in Molecular Cell (Hoeller et al., 2007) now describes the E3-independent monoubiquitination of certain proteins. The mechanism has interesting parallels to SUMO ligation.

Publication types

Review

MeSH terms

Endocytosis / physiology*
Humans
Ubiquitin / metabolism*
Ubiquitin-Protein Ligases

Substances

Ubiquitin
Ubiquitin-Protein Ligases