Characterization of a p53 Regulatory Domain
Abstract
A putative domain may be present within p53 involving its regulation. Further evidence of a regulatory domain is derived from a comparison of p53 with two oncogenes, c-jun and c-fos. Amino acids 93-160 from p53 show a significant homology to c-jun and c-fos inhibitory domains, especially to c-jun's 8 region. The c-jun 8 region has been found to play an inhibitory role by interacting with a member of the. MAPK family, JNK. Once bound to c-jun, JNK is capable of phosphorylating serine residues 63 and %3. Two conserved serine residues within p53,s potential regulatory domain may also be involved in phosphorylation and regulation. Therefore, we hypothesized that p53 serine residues 116 and 127, homologous to c-jun serine residues 63 and 73, may be phosphorylated by JNK or another MAPK family member.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2001
- Accession Number
- ADA405271
Entities
People
- Brian C. Abela
- Kuan Liu
Organizations
- University of California, Riverside