Cullin 5 Expression in the Rat: Cellular and Tissue Distribution, and Changes in Response to Water Deprivation and Hemorrhagic Shock
Abstract
Protein degradation by ubiquitination and the 26S proteasome is used to modulate the steady-state levels of proteins and to regulate cellular processes. Proteins become targets of the proteasome by covalent attachment of polyubiquitin chains, which requires three main enzymes (E1, E2, and E3). It is the E3 ubiquitin ligases that control the selection and specificity of substrate ubiquitination. Cullin-5 (Cul-5), a member of the cullin family of E3 ubiquitin ligases, remains obscure. The goals of this research project were to characterize Cul-5, and investigate its response to cellular stresses of water deprivation and hemorrhagic shock in the rat.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 28, 2003
- Accession Number
- ADA421696
Entities
People
- Thomas E. Ceremuga
Organizations
- Uniformed Services University of the Health Sciences