Structural complexity in ubiquitin recognition

J Wade Harper; Brenda A Schulman

doi:10.1016/j.cell.2006.03.009

Structural complexity in ubiquitin recognition

Cell. 2006 Mar 24;124(6):1133-6. doi: 10.1016/j.cell.2006.03.009.

Authors

J Wade Harper¹, Brenda A Schulman

Affiliation

¹ Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. wade_harper@hms.harvard.edu

PMID: 16564007
DOI: 10.1016/j.cell.2006.03.009

Abstract

Ubiquitinated proteins are sorted into distinct pathways via association with several classes of ubiquitin binding domain-containing proteins. A virtual explosion in the field of ubiquitin binding proteins has revealed several new classes and interactions with distinct surfaces on ubiquitin, providing a clearer understanding of how sorting of ubiquitinated proteins is achieved.

Publication types

Review

MeSH terms

Animals
Guanine Nucleotide Exchange Factors / chemistry
Guanine Nucleotide Exchange Factors / metabolism*
Humans
Models, Molecular
Protein Binding
Protein Structure, Tertiary / physiology
Protein Transport
Signal Transduction / physiology*
Ubiquitin / chemistry
Ubiquitin / metabolism*

Substances

Guanine Nucleotide Exchange Factors
RABGEF1 protein, human
Ubiquitin

Grants and funding

R01 AG011085/AG/NIA NIH HHS/United States