p23, a simple protein with complex activities
AUTOR(ES)
Felts, Sara J.
FONTE
Cell Stress Society International
RESUMO
p23 is a small but important cochaperone for the Hsp90 chaperoning pathway. It appears to facilitate the adenosine triphosphate–driven cycle of Hsp90 binding to client proteins. It enters at a late stage of the cycle and enhances the maturation of client proteins. Although this role of p23 is fairly well established, recent studies suggest that it may have additional functions in the cell that merit further exploration.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=514861Documentos Relacionados
- p23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway
- A mutation in P23, the first gene in the RNA polymerase sigma A (sigma 43) operon, affects sporulation in Bacillus subtilis.
- Characterization of the Mitochondrial Inner Membrane Translocase Complex: the Tim23p Hydrophobic Domain Interacts with Tim17p but Not with Other Tim23p Molecules
- The Saccharomyces cerevisiae Homologue of Human Wiskott–Aldrich Syndrome Protein Las17p Interacts with the Arp2/3 Complex
- ATPase and GTPase Activities Associated with a Specific 5S RNA-Protein Complex*