Identification of Novel Human Cdt1-binding Proteins by a Proteomics Approach: Proteolytic Regulation by APC/CCdh1
Immunoprecipitation
DOI:
10.1091/mbc.e07-09-0859
Publication Date:
2007-12-28T01:34:19Z
AUTHORS (9)
ABSTRACT
In mammalian cells, Cdt1 activity is strictly controlled by multiple independent mechanisms, implying that it central to the regulation of DNA replication during cell cycle. fact, unscheduled hyperfunction results in rereplication and/or chromosomal damage. Thus, important understand its function and regulations precisely. We sought comprehensively identify human Cdt1-binding proteins a combination affinity chromatography liquid tandem mass spectrometry analysis. Through this approach, we could newly 11 proteins, including subunits anaphase-promoting complex/cyclosome (APC/C), SNF2H WSTF, topoisomerase I IIalpha, GRWD1/WDR28, nucleophosmin/nucleoplasmin, importins. vivo interactions with APC/C(Cdh1), SNF2H, GRWD1/WDR28 were confirmed coimmunoprecipitation assays. A further focus on APC/C(Cdh1) indicated ubiquitin ligase controls levels cycle via three destruction boxes N-terminus. Notably, elimination these resulted induction strong addition SCF(Skp2) cullin4-based ligases, third plays crucial role proteolytic cells.
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (69)
CITATIONS (58)
EXTERNAL LINKS
PlumX Metrics
RECOMMENDATIONS
FAIR ASSESSMENT
Coming soon ....
JUPYTER LAB
Coming soon ....