122 |
Entry URI |
http://metadb.riken.jp/db/SciNetS_ria224i/cria224u4ria224u15498773i |
Entry name |
Rancour David M et al. 2004 Dec. J. Biol. Chem. 279(52):54264-74. |
Title |
Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric structure and activity of arabidopsis CDC48. |
Authors |
Bednarek Sebastian Y|Knight Seth D|Park Sookhee|Rancour David M |
Abstract |
p97/CDC48 is a highly abundant hexameric AAA-ATPase that functions as a molecular chaperone in numerous diverse cellular activities. We have identified an Arabidopsis UBX domain-containing protein, PUX1, which functions to regulate the oligomeric structure of the Arabidopsis homolog of p97/CDC48, AtCDC48, as well as mammalian p97. PUX1 is a soluble protein that co-fractionates with non-hexameric AtCDC48 and physically interacts with AtCDC48 in vivo. Binding of PUX1 to AtCDC48 is mediated through the UBX-containing C-terminal domain. However, disassembly of the chaperone is dependent upon the N-terminal domain of PUX1. These findings provide evidence that the assembly and disassembly of the hexameric p97/CDC48 complex is a dynamic process. This new unexpected level of regulation for p97/CDC48 was demonstrated to be critical in vivo as pux1 loss-of-function mutants display accelerated growth relative to wild-type plants. These results suggest a role for AtCDC48 and PUX1 in regulating plant growth. |
Pubmed ID |
15498773 |
Journal |
The Journal of biological chemistry |
Volume |
279 |
Issue |
52 |
Pages |
54264-74 |
Publication date |
2004 Dec |
Num of phenotype gene |
1 |