Twice primed: cyclin E is phosphorylated and isomerized before being ubiquitinated

Stuart D Shumway; Yue Xiong

doi:10.1016/j.molcel.2006.07.002

Twice primed: cyclin E is phosphorylated and isomerized before being ubiquitinated

Mol Cell. 2006 Jul 21;23(2):149-50. doi: 10.1016/j.molcel.2006.07.002.

Authors

Stuart D Shumway¹, Yue Xiong

Affiliation

¹ Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.

PMID: 16857579
DOI: 10.1016/j.molcel.2006.07.002

Abstract

Targeting proteins for irreversible degradation must be under tight control and is often regulated at the level of substrate-receptor binding. But does a protein really need to be marked twice with two different modifications, first phosphorylation and then isomerization, to bind its receptor, as van Drogen et al. (2006) show for cyclin E?

Publication types

Review
Comment

MeSH terms

Cell Cycle Proteins / metabolism
Cyclin E / agonists*
Cyclin E / metabolism*
F-Box Proteins / metabolism
Isomerism
Phosphorylation
Protein Binding
Ubiquitin-Protein Ligases / metabolism
Ubiquitins / metabolism*

Substances

Cell Cycle Proteins
Cyclin E
F-Box Proteins
Ubiquitins
Ubiquitin-Protein Ligases